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- PDB-7mns: Crystal Structure of the ZnF4 of Nucleoporin NUP358/RanBP2 in com... -

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Entry
Database: PDB / ID: 7mns
TitleCrystal Structure of the ZnF4 of Nucleoporin NUP358/RanBP2 in complex with Ran-GDP
Components
  • E3 SUMO-protein ligase RanBP2
  • GTP-binding nuclear protein Ran
KeywordsTRANSPORT PROTEIN / NUCLEAR PORE COMPLEX COMPONENT / NUCLEOCYTOPLASMIC TRANSPORT / ZINC FINGER
Function / homology
Function and homology information


cytoplasmic periphery of the nuclear pore complex / SUMO ligase complex / SUMO ligase activity / annulate lamellae / RNA nuclear export complex / nuclear pore cytoplasmic filaments / pre-miRNA export from nucleus / snRNA import into nucleus / Nuclear Pore Complex (NPC) Disassembly / manchette ...cytoplasmic periphery of the nuclear pore complex / SUMO ligase complex / SUMO ligase activity / annulate lamellae / RNA nuclear export complex / nuclear pore cytoplasmic filaments / pre-miRNA export from nucleus / snRNA import into nucleus / Nuclear Pore Complex (NPC) Disassembly / manchette / nuclear inclusion body / cellular response to mineralocorticoid stimulus / nuclear pore nuclear basket / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / Regulation of cholesterol biosynthesis by SREBP (SREBF) / importin-alpha family protein binding / Transport of the SLBP independent Mature mRNA / Transport of the SLBP Dependant Mature mRNA / NS1 Mediated Effects on Host Pathways / SUMOylation of SUMOylation proteins / Transport of Mature mRNA Derived from an Intronless Transcript / protein localization to nucleolus / Rev-mediated nuclear export of HIV RNA / Transferases; Acyltransferases; Aminoacyltransferases / Nuclear import of Rev protein / nuclear export / SUMOylation of RNA binding proteins / NEP/NS2 Interacts with the Cellular Export Machinery / GTP metabolic process / SUMO transferase activity / tRNA processing in the nucleus / Transport of Mature mRNA derived from an Intron-Containing Transcript / Postmitotic nuclear pore complex (NPC) reformation / MicroRNA (miRNA) biogenesis / nucleocytoplasmic transport / Viral Messenger RNA Synthesis / centrosome localization / DNA metabolic process / dynein intermediate chain binding / NLS-bearing protein import into nucleus / regulation of gluconeogenesis / SUMOylation of ubiquitinylation proteins / Vpr-mediated nuclear import of PICs / mitotic sister chromatid segregation / SUMOylation of DNA replication proteins / protein sumoylation / spermatid development / ribosomal large subunit export from nucleus / Regulation of HSF1-mediated heat shock response / sperm flagellum / mRNA transport / viral process / nuclear pore / ribosomal subunit export from nucleus / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / ribosomal small subunit export from nucleus / SUMOylation of DNA damage response and repair proteins / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / Resolution of Sister Chromatid Cohesion / protein export from nucleus / centriole / response to amphetamine / SUMOylation of chromatin organization proteins / mitotic spindle organization / HCMV Late Events / male germ cell nucleus / hippocampus development / RHO GTPases Activate Formins / Transcriptional regulation by small RNAs / recycling endosome / G protein activity / ISG15 antiviral mechanism / small GTPase binding / positive regulation of protein import into nucleus / HCMV Early Events / protein import into nucleus / Separation of Sister Chromatids / GDP binding / Signaling by ALK fusions and activated point mutants / melanosome / positive regulation of protein binding / protein folding / nuclear envelope / mitotic cell cycle / snRNP Assembly / midbody / actin cytoskeleton organization / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / nuclear membrane / cadherin binding / protein heterodimerization activity / protein domain specific binding / cell division / intracellular membrane-bounded organelle / GTPase activity / chromatin binding / protein-containing complex binding
Similarity search - Function
Nup358/RanBP2 E3 ligase domain / Nup358/RanBP2 E3 ligase domain / Ran binding domain / Ran binding protein RanBP1-like / RanBP1 domain / Ran binding domain type 1 profile. / Ran-binding domain / small GTPase Ran family profile. / Ran GTPase / Zinc finger domain ...Nup358/RanBP2 E3 ligase domain / Nup358/RanBP2 E3 ligase domain / Ran binding domain / Ran binding protein RanBP1-like / RanBP1 domain / Ran binding domain type 1 profile. / Ran-binding domain / small GTPase Ran family profile. / Ran GTPase / Zinc finger domain / Zn-finger in Ran binding protein and others / Zinc finger RanBP2 type profile. / Zinc finger RanBP2-type signature. / Zinc finger, RanBP2-type superfamily / Zinc finger, RanBP2-type / Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site / Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain profile. / Cyclophilin-type peptidyl-prolyl cis-trans isomerase domain / Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD / Cyclophilin-like domain superfamily / Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases / TPR repeat region circular profile. / TPR repeat profile. / Tetratricopeptide repeats / Tetratricopeptide repeat / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / Small GTP-binding protein domain / Tetratricopeptide-like helical domain superfamily / PH-like domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / E3 SUMO-protein ligase RanBP2 / GTP-binding nuclear protein Ran
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 2.1 Å
AuthorsBley, C.J. / Nie, S. / Mobbs, G.W. / Petrovic, S. / Gres, A.T. / Liu, X. / Mukherjee, S. / Harvey, S. / Huber, F.M. / Lin, D.H. ...Bley, C.J. / Nie, S. / Mobbs, G.W. / Petrovic, S. / Gres, A.T. / Liu, X. / Mukherjee, S. / Harvey, S. / Huber, F.M. / Lin, D.H. / Brown, B. / Tang, A.W. / Rundlet, E.J. / Correia, A.R. / Chen, S. / Regmi, S.G. / Stevens, T.A. / Jette, C.A. / Dasso, M. / Patke, A. / Palazzo, A.F. / Kossiakoff, A.A. / Hoelz, A.
Funding support United States, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM117360 United States
Howard Hughes Medical Institute (HHMI)55108534 United States
Heritage Medical Research Institute United States
CitationJournal: Science / Year: 2022
Title: Architecture of the cytoplasmic face of the nuclear pore.
Authors: Christopher J Bley / Si Nie / George W Mobbs / Stefan Petrovic / Anna T Gres / Xiaoyu Liu / Somnath Mukherjee / Sho Harvey / Ferdinand M Huber / Daniel H Lin / Bonnie Brown / Aaron W Tang / ...Authors: Christopher J Bley / Si Nie / George W Mobbs / Stefan Petrovic / Anna T Gres / Xiaoyu Liu / Somnath Mukherjee / Sho Harvey / Ferdinand M Huber / Daniel H Lin / Bonnie Brown / Aaron W Tang / Emily J Rundlet / Ana R Correia / Shane Chen / Saroj G Regmi / Taylor A Stevens / Claudia A Jette / Mary Dasso / Alina Patke / Alexander F Palazzo / Anthony A Kossiakoff / André Hoelz /
Abstract: INTRODUCTION The subcellular compartmentalization of eukaryotic cells requires selective transport of folded proteins and protein-nucleic acid complexes. Embedded in nuclear envelope pores, which are ...INTRODUCTION The subcellular compartmentalization of eukaryotic cells requires selective transport of folded proteins and protein-nucleic acid complexes. Embedded in nuclear envelope pores, which are generated by the circumscribed fusion of the inner and outer nuclear membranes, nuclear pore complexes (NPCs) are the sole bidirectional gateways for nucleocytoplasmic transport. The ~110-MDa human NPC is an ~1000-protein assembly that comprises multiple copies of ~34 different proteins, collectively termed nucleoporins. The symmetric core of the NPC is composed of an inner ring encircling the central transport channel and outer rings formed by Y‑shaped coat nucleoporin complexes (CNCs) anchored atop both sides of the nuclear envelope. The outer rings are decorated with compartment‑specific asymmetric nuclear basket and cytoplasmic filament nucleoporins, which establish transport directionality and provide docking sites for transport factors and the small guanosine triphosphatase Ran. The cytoplasmic filament nucleoporins also play an essential role in the irreversible remodeling of messenger ribonucleoprotein particles (mRNPs) as they exit the central transport channel. Unsurprisingly, the NPC's cytoplasmic face represents a hotspot for disease‑associated mutations and is commonly targeted by viral virulence factors. RATIONALE Previous studies established a near-atomic composite structure of the human NPC's symmetric core by combining (i) biochemical reconstitution to elucidate the interaction network between symmetric nucleoporins, (ii) crystal and single-particle cryo-electron microscopy structure determination of nucleoporins and nucleoporin complexes to reveal their three-dimensional shape and the molecular details of their interactions, (iii) quantitative docking in cryo-electron tomography (cryo-ET) maps of the intact human NPC to uncover nucleoporin stoichiometry and positioning, and (iv) cell‑based assays to validate the physiological relevance of the biochemical and structural findings. In this work, we extended our approach to the cytoplasmic filament nucleoporins to reveal the near-atomic architecture of the cytoplasmic face of the human NPC. RESULTS Using biochemical reconstitution, we elucidated the protein-protein and protein-RNA interaction networks of the human and cytoplasmic filament nucleoporins, establishing an evolutionarily conserved heterohexameric cytoplasmic filament nucleoporin complex (CFNC) held together by a central heterotrimeric coiled‑coil hub that tethers two separate mRNP‑remodeling complexes. Further biochemical analysis and determination of a series of crystal structures revealed that the metazoan‑specific cytoplasmic filament nucleoporin NUP358 is composed of 16 distinct domains, including an N‑terminal S‑shaped α‑helical solenoid followed by a coiled‑coil oligomerization element, numerous Ran‑interacting domains, an E3 ligase domain, and a C‑terminal prolyl‑isomerase domain. Physiologically validated quantitative docking into cryo-ET maps of the intact human NPC revealed that pentameric NUP358 bundles, conjoined by the oligomerization element, are anchored through their N‑terminal domains to the central stalk regions of the CNC, projecting flexibly attached domains as far as ~600 Å into the cytoplasm. Using cell‑based assays, we demonstrated that NUP358 is dispensable for the architectural integrity of the assembled interphase NPC and RNA export but is required for efficient translation. After NUP358 assignment, the remaining 4-shaped cryo‑ET density matched the dimensions of the CFNC coiled‑coil hub, in close proximity to an outer-ring NUP93. Whereas the N-terminal NUP93 assembly sensor motif anchors the properly assembled related coiled‑coil channel nucleoporin heterotrimer to the inner ring, biochemical reconstitution confirmed that the NUP93 assembly sensor is reused in anchoring the CFNC to the cytoplasmic face of the human NPC. By contrast, two CFNCs are anchored by a divergent mechanism that involves assembly sensors located in unstructured portions of two CNC nucleoporins. Whereas unassigned cryo‑ET density occupies the NUP358 and CFNC binding sites on the nuclear face, docking of the nuclear basket component ELYS established that the equivalent position on the cytoplasmic face is unoccupied, suggesting that mechanisms other than steric competition promote asymmetric distribution of nucleoporins. CONCLUSION We have substantially advanced the biochemical and structural characterization of the asymmetric nucleoporins' architecture and attachment at the cytoplasmic and nuclear faces of the NPC. Our near‑atomic composite structure of the human NPC's cytoplasmic face provides a biochemical and structural framework for elucidating the molecular basis of mRNP remodeling, viral virulence factor interference with NPC function, and the underlying mechanisms of nucleoporin diseases at the cytoplasmic face of the NPC. [Figure: see text].
History
DepositionMay 1, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 15, 2022Provider: repository / Type: Initial release
Revision 1.1Jun 22, 2022Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: GTP-binding nuclear protein Ran
B: E3 SUMO-protein ligase RanBP2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)31,8015
Polymers31,2682
Non-polymers5333
Water2,864159
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration, SEC-MALS
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2530 Å2
ΔGint-29 kcal/mol
Surface area11720 Å2
MethodPISA
Unit cell
Length a, b, c (Å)92.480, 92.480, 194.780
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number179
Space group name H-MP6522
Components on special symmetry positions
IDModelComponents
11A-533-

HOH

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Components

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Protein / Protein/peptide , 2 types, 2 molecules AB

#1: Protein GTP-binding nuclear protein Ran / Androgen receptor-associated protein 24 / GTPase Ran / Ras-like protein TC4 / Ras-related nuclear protein


Mass: 26567.381 Da / Num. of mol.: 1 / Mutation: F35S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RAN, ARA24, OK/SW-cl.81 / Production host: Escherichia coli (E. coli) / References: UniProt: P62826
#2: Protein/peptide E3 SUMO-protein ligase RanBP2 / 358 kDa nucleoporin / Nuclear pore complex protein Nup358 / Nucleoporin Nup358 / Ran-binding ...358 kDa nucleoporin / Nuclear pore complex protein Nup358 / Nucleoporin Nup358 / Ran-binding protein 2 / RanBP2 / p270


Mass: 4700.296 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RANBP2, NUP358 / Production host: Escherichia coli (E. coli) / References: UniProt: P49792

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Non-polymers , 4 types, 162 molecules

#3: Chemical ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#4: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#5: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Zn
#6: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 159 / Source method: isolated from a natural source / Formula: H2O

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Details

Has ligand of interestN

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 3.84 Å3/Da / Density % sol: 68.01 %
Crystal growTemperature: 294 K / Method: vapor diffusion, hanging drop / pH: 6.5 / Details: 18 % (w/v) PEG 3,350; 0.1M Bis-Tris

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 1.2821 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 13, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.2821 Å / Relative weight: 1
ReflectionResolution: 2.1→29.91 Å / Num. obs: 29596 / % possible obs: 100 % / Redundancy: 25.5 % / Biso Wilson estimate: 32.46 Å2 / Rpim(I) all: 0.035 / Rrim(I) all: 0.181 / Net I/σ(I): 21.2 / Num. measured all: 754508
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. measured allNum. unique obsRpim(I) allRrim(I) all% possible all
2.1-2.1825.81.87390528600.4482.31599.9
4.52-29.9223.464.47584532460.010.052100

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Processing

Software
NameVersionClassification
xia2data scaling
PHENIX1.18.2refinement
PDB_EXTRACT3.27data extraction
Cootmodel building
AutoSolphasing
XDSdata processing
XDSdata reduction
RefinementMethod to determine structure: SAD / Resolution: 2.1→29.91 Å / SU ML: 0.2 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 18.32 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2025 1477 5 %
Rwork0.1747 28049 -
obs0.1761 29526 99.97 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 188.95 Å2 / Biso mean: 53.0976 Å2 / Biso min: 23.93 Å2
Refinement stepCycle: final / Resolution: 2.1→29.91 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1909 0 42 159 2110
Biso mean--37.52 50.62 -
Num. residues----240
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 11 / % reflection obs: 100 %

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all
2.1-2.170.26811410.246724612602
2.17-2.250.21221520.205224772629
2.25-2.340.23041100.183325132623
2.34-2.440.22321250.187725162641
2.44-2.570.20991280.173625242652
2.57-2.730.2121140.169725282642
2.73-2.940.1991420.170925112653
2.94-3.240.22311340.173125552689
3.24-3.710.21471560.162925582714
3.71-4.670.15791370.146526142751
4.67-29.910.20611380.195427922930
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
12.3091-0.28740.32192.8694-0.25820.5914-0.04090.12250.06830.0713-0.0691-0.0122-0.0694-0.18210.10550.25360.01270.03790.3287-0.03750.319432.387443.3279100.3596
22.9254-0.18180.10232.0634-0.710.84640.10180.2171-0.2275-0.0666-0.00740.12230.1401-0.0567-0.06210.2692-0.00090.02750.3405-0.0380.311827.960743.6163101.0801
33.1288-1.099-2.22761.48581.95553.00160.26890.32260.3079-0.3233-0.1768-0.2646-0.5099-0.1972-0.09850.40180.03130.06620.36840.02950.335435.66850.881192.3819
44.71543.11330.55826.789-1.75184.26810.06280.2276-0.1291-0.3247-0.3872-0.8548-0.10730.63830.22380.32420.04810.10150.56450.00790.481650.740340.899489.4943
53.7409-0.177-0.14022.506-0.25774.10440.0098-0.12840.18060.0948-0.0857-0.4415-0.12510.26930.07510.2347-0.02570.02740.3639-0.03280.382244.474743.7168100.3943
69.3357-3.13310.21593.21633.47857.6009-0.3368-0.2809-0.452-0.02030.0524-0.3807-0.66660.62830.32120.2712-0.10090.01570.3344-0.02210.374242.365751.0513108.1543
71.691-1.2174-0.94830.8150.40471.56180.0201-0.1484-0.11720.16420.0222-0.29520.04970.3968-0.02110.2785-0.03990.00790.3324-0.00020.370146.75537.5927104.7193
87.142-5.3662.26454.2391-0.99343.0697-0.6952-0.19611.11780.4990.1337-0.7288-1.14950.44170.31080.8036-0.0335-0.26570.6781-0.10631.479658.030849.358197.7891
99.25843.21291.82784.89274.10563.5499-0.7844-0.02791.66070.0793-0.5926-0.1936-1.21330.33831.13391.30580.0945-0.06350.8581-0.04520.910637.133454.2599121.3688
105.4529-3.55-4.38682.72352.64113.65060.1523-1.82650.56330.5737-0.7036-0.6193-1.02710.46750.25680.75070.05090.11360.9224-0.25531.89432.025258.4603116.4315
113.9608-2.22211.83584.40223.69348.71970.55610.2408-0.2719-0.08540.4719-1.57360.06660.8929-0.93860.60660.0946-0.00610.6239-0.18210.600822.244361.5798115.7784
122.1609-0.8894-0.19823.71820.9752.8279-0.0711-0.10630.22240.32020.07970.1346-0.53190.0556-0.02950.40280.04720.0570.3731-0.02260.365217.653556.643106.1212
134.46271.10672.96865.70334.30734.32790.3911-0.98880.53110.7422-0.61271.12520.5147-0.3720.38050.4738-0.04790.05040.4144-0.05840.505111.716452.83103.7315
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 7 through 29 )A7 - 29
2X-RAY DIFFRACTION2chain 'A' and (resid 30 through 73 )A30 - 73
3X-RAY DIFFRACTION3chain 'A' and (resid 74 through 123 )A74 - 123
4X-RAY DIFFRACTION4chain 'A' and (resid 124 through 139 )A124 - 139
5X-RAY DIFFRACTION5chain 'A' and (resid 140 through 161 )A140 - 161
6X-RAY DIFFRACTION6chain 'A' and (resid 162 through 168 )A162 - 168
7X-RAY DIFFRACTION7chain 'A' and (resid 169 through 201 )A169 - 201
8X-RAY DIFFRACTION8chain 'A' and (resid 202 through 208 )A202 - 208
9X-RAY DIFFRACTION9chain 'B' and (resid 1534 through 1537 )B0
10X-RAY DIFFRACTION10chain 'B' and (resid 1538 through 1541 )B0
11X-RAY DIFFRACTION11chain 'B' and (resid 1542 through 1545 )B0
12X-RAY DIFFRACTION12chain 'B' and (resid 1546 through 1566 )B0
13X-RAY DIFFRACTION13chain 'B' and (resid 1567 through 1571 )B0

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