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- PDB-2v55: Mechanism of multi-site phosphorylation from a ROCK-I:RhoE comple... -

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Basic information

Entry
Database: PDB / ID: 2v55
TitleMechanism of multi-site phosphorylation from a ROCK-I:RhoE complex structure
Components
  • RHO-ASSOCIATED PROTEIN KINASE 1
  • RHO-RELATED GTP-BINDING PROTEIN RHOE
KeywordsTRANSFERASE / SERINE/THREONINE-PROTEIN KINASE / RHOE / ZINC / KINASE / ROCK-I / MEMBRANE / APOPTOSIS / CYTOPLASM / G-PROTEINS / METHYLATION / ZINC-FINGER / NUCLEOTIDE-BINDING / PHORBOL-ESTER BINDING / ATP-BINDING / PRENYLATION / LIPOPROTEIN / MULTI-SITE PHOSPHORYLATION / COILED COIL / GTP-BINDING / POLYMORPHISM / STRESS FIBRES / METAL-BINDING / PHOSPHOPROTEIN / GOLGI APPARATUS
Function / homology
Function and homology information


myoblast migration / podocyte cell migration / regulation of angiotensin-activated signaling pathway / ROCK-subfamily protein kinase / membrane to membrane docking / regulation of keratinocyte differentiation / Rho-dependent protein serine/threonine kinase activity / negative regulation of membrane protein ectodomain proteolysis / response to transforming growth factor beta / positive regulation of connective tissue replacement ...myoblast migration / podocyte cell migration / regulation of angiotensin-activated signaling pathway / ROCK-subfamily protein kinase / membrane to membrane docking / regulation of keratinocyte differentiation / Rho-dependent protein serine/threonine kinase activity / negative regulation of membrane protein ectodomain proteolysis / response to transforming growth factor beta / positive regulation of connective tissue replacement / regulation of cell junction assembly / negative regulation of amyloid precursor protein catabolic process / smooth muscle contraction / embryonic morphogenesis / positive regulation of amyloid-beta clearance / regulation of cell motility / leukocyte tethering or rolling / neuron projection arborization / response to angiotensin / bleb / negative regulation of biomineral tissue development / regulation of establishment of endothelial barrier / regulation of synapse maturation / regulation of stress fiber assembly / RHO GTPases Activate ROCKs / actomyosin structure organization / Sema4D induced cell migration and growth-cone collapse / cortical actin cytoskeleton organization / aortic valve morphogenesis / RND3 GTPase cycle / regulation of neuron differentiation / leukocyte migration / regulation of focal adhesion assembly / RHOBTB1 GTPase cycle / RHOB GTPase cycle / tau-protein kinase activity / leukocyte cell-cell adhesion / EPHA-mediated growth cone collapse / Apoptotic cleavage of cellular proteins / regulation of establishment of cell polarity / positive regulation of cardiac muscle hypertrophy / negative regulation of bicellular tight junction assembly / mRNA destabilization / small GTPase-mediated signal transduction / RHOC GTPase cycle / negative regulation of amyloid-beta formation / mitotic cytokinesis / epithelial to mesenchymal transition / RHOH GTPase cycle / Rho protein signal transduction / positive regulation of focal adhesion assembly / RHOA GTPase cycle / regulation of cell adhesion / negative regulation of protein binding / regulation of synaptic vesicle endocytosis / ruffle / negative regulation of angiogenesis / EPHB-mediated forward signaling / centriole / regulation of cell migration / positive regulation of autophagy / blood vessel diameter maintenance / protein localization to plasma membrane / actin filament organization / regulation of actin cytoskeleton organization / small monomeric GTPase / regulation of microtubule cytoskeleton organization / peptidyl-serine phosphorylation / VEGFA-VEGFR2 Pathway / tau protein binding / Schaffer collateral - CA1 synapse / small GTPase binding / neuron projection development / cytoplasmic stress granule / actin cytoskeleton organization / lamellipodium / G alpha (12/13) signalling events / secretory granule lumen / Potential therapeutics for SARS / cytoskeleton / positive regulation of MAPK cascade / cell adhesion / intracellular signal transduction / Golgi membrane / protein serine kinase activity / focal adhesion / protein serine/threonine kinase activity / apoptotic process / positive regulation of gene expression / GTPase activity / Neutrophil degranulation / protein kinase binding / GTP binding / signal transduction / extracellular region / zinc ion binding / ATP binding / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Rho-related GTP-binding protein RhoE / Rho-associated protein kinase 1, HR1 / ROCK, Rho binding domain / Rho-associated protein kinase 1/2 / Rho Binding / Rho-binding (RhoBD) domain profile. / : / MRCK kinase PH domain / : / HR1 rho-binding domain ...Rho-related GTP-binding protein RhoE / Rho-associated protein kinase 1, HR1 / ROCK, Rho binding domain / Rho-associated protein kinase 1/2 / Rho Binding / Rho-binding (RhoBD) domain profile. / : / MRCK kinase PH domain / : / HR1 rho-binding domain / REM-1 domain profile. / Small GTPase Rho / Small GTPase Rho domain profile. / Zinc finger phorbol-ester/DAG-type profile. / Protein kinase C conserved region 1 (C1) domains (Cysteine-rich domains) / Protein kinase C-like, phorbol ester/diacylglycerol-binding domain / C1-like domain superfamily / Extension to Ser/Thr-type protein kinases / AGC-kinase, C-terminal / AGC-kinase C-terminal domain profile. / PH domain profile. / Pleckstrin homology domain. / Pleckstrin homology domain / 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 / PH-like domain superfamily / P-loop containing nucleotide triphosphate hydrolases / Phosphorylase Kinase; domain 1 / Phosphorylase Kinase; domain 1 / Transferase(Phosphotransferase) domain 1 / Transferase(Phosphotransferase); domain 1 / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 2-Layer Sandwich / Orthogonal Bundle / 3-Layer(aba) Sandwich / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / GUANOSINE-5'-TRIPHOSPHATE / Rho-related GTP-binding protein RhoE / Rho-associated protein kinase 1
Similarity search - Component
Biological speciesHOMO SAPIENS (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.705 Å
AuthorsKomander, D. / Garg, R. / Wan, P.T.C. / Ridley, A.J. / Barford, D.
CitationJournal: Embo J. / Year: 2008
Title: Mechanism of Multi-Site Phosphorylation from a Rock-I:Rhoe Complex Structure.
Authors: Komander, D. / Garg, R. / Wan, P.T.C. / Ridley, A.J. / Barford, D.
History
DepositionOct 1, 2008Deposition site: PDBE / Processing site: PDBE
Revision 1.0Nov 4, 2008Provider: repository / Type: Initial release
Revision 1.1May 8, 2011Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Dec 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Other / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_database_status / pdbx_initial_refinement_model / pdbx_struct_conn_angle / struct_conn
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_sf / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _struct_conn.pdbx_dist_value / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id
Remark 700 SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED.

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: RHO-ASSOCIATED PROTEIN KINASE 1
B: RHO-RELATED GTP-BINDING PROTEIN RHOE
C: RHO-ASSOCIATED PROTEIN KINASE 1
D: RHO-RELATED GTP-BINDING PROTEIN RHOE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)141,14713
Polymers138,8954
Non-polymers2,2529
Water00
1
A: RHO-ASSOCIATED PROTEIN KINASE 1
B: RHO-RELATED GTP-BINDING PROTEIN RHOE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,5266
Polymers69,4482
Non-polymers1,0784
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1830 Å2
ΔGint-6.1 kcal/mol
Surface area33100 Å2
MethodPQS
2
C: RHO-ASSOCIATED PROTEIN KINASE 1
D: RHO-RELATED GTP-BINDING PROTEIN RHOE
hetero molecules


Theoretical massNumber of molelcules
Total (without water)70,6227
Polymers69,4482
Non-polymers1,1745
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area1840 Å2
ΔGint-6.5 kcal/mol
Surface area33820 Å2
MethodPQS
Unit cell
Length a, b, c (Å)152.477, 152.477, 531.274
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number179
Space group name H-MP6522
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-ID
11
21
12
22

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection details
111CHAIN A AND (RESSEQ 6:371 OR RESSEQ 378:404 OR RESSEQ 1480:1481 )
211CHAIN C AND (RESSEQ 6:371 OR RESSEQ 375:404 OR RESSEQ 1480:1481 )
112CHAIN B AND (RESSEQ 20:200 OR RESSEQ 1201:1202 )
212CHAIN D AND (RESSEQ 20:200 OR RESSEQ 1201:1202 )

NCS ensembles :
ID
1
2

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Components

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Protein , 2 types, 4 molecules ACBD

#1: Protein RHO-ASSOCIATED PROTEIN KINASE 1 / ROCK1 / RHO-ASSOCIATED / COILED-COIL-CONTAINING PROTEIN KINASE 1 / P160 ROCK-1 / P160ROCK / RENAL ...ROCK1 / RHO-ASSOCIATED / COILED-COIL-CONTAINING PROTEIN KINASE 1 / P160 ROCK-1 / P160ROCK / RENAL CARCINOMA ANTIGEN NY-REN-35


Mass: 47020.234 Da / Num. of mol.: 2 / Fragment: KINASE DOMAIN, RESIDUES 1-406
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PHTB / Cell line (production host): SF9 / Production host: SPODOPTERA FRUGIPERDA (fall armyworm)
References: UniProt: Q13464, non-specific serine/threonine protein kinase
#2: Protein RHO-RELATED GTP-BINDING PROTEIN RHOE / RHOE / RHO FAMILY GTPASE 3 / RND3 / RHO8 / MEMB PROTEIN


Mass: 22427.449 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-200
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET28 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P61587

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Non-polymers , 4 types, 9 molecules

#3: Chemical ChemComp-ANP / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER


Mass: 506.196 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H17N6O12P3 / Comment: AMP-PNP, energy-carrying molecule analogue*YM
#4: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#5: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE


Mass: 523.180 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Comment: GTP, energy-carrying molecule*YM
#6: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4

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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: 6.3 Å3/Da / Density % sol: 85 % / Description: NONE
Crystal growpH: 6.5
Details: 0.6 - 1 M NA/K TARTRATE, 0.1 M MES [PH 5-6], 0.2 M LISO4

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 1
DetectorType: ADSC CCD / Detector: CCD / Date: Feb 18, 2007
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.7→131 Å / Num. obs: 39411 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 3.8 % / Biso Wilson estimate: 74.95 Å2 / Rmerge(I) obs: 0.19 / Net I/σ(I): 8.4
Reflection shellResolution: 3.7→3.9 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 3 / % possible all: 99.9

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE)refinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRIES 2ETR AND 1GWN

2etr

1gwn


Resolution: 3.705→49.288 Å / SU ML: 0.5 / σ(F): 1.36 / Phase error: 21.4 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2689 809 2.06 %
Rwork0.2376 --
obs0.2382 39321 98.31 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 55.719 Å2 / ksol: 0.345 e/Å3
Displacement parametersBiso mean: 81.67 Å2
Baniso -1Baniso -2Baniso -3
1-1.6465 Å20 Å20 Å2
2--1.6465 Å2-0 Å2
3----3.2931 Å2
Refinement stepCycle: LAST / Resolution: 3.705→49.288 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9053 0 135 0 9188
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d09397
X-RAY DIFFRACTIONf_angle_d1.312791
X-RAY DIFFRACTIONf_dihedral_angle_d23.233370
X-RAY DIFFRACTIONf_chiral_restr0.081398
X-RAY DIFFRACTIONf_plane_restr01636
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDTypeRms dev position (Å)
11A3082X-RAY DIFFRACTIONPOSITIONAL
12C3082X-RAY DIFFRACTIONPOSITIONAL0.049
21B1366X-RAY DIFFRACTIONPOSITIONAL
22D1366X-RAY DIFFRACTIONPOSITIONAL0.044
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.7049-3.9370.31641180.27936307X-RAY DIFFRACTION99
3.937-4.24080.2641390.25196395X-RAY DIFFRACTION100
4.2408-4.66730.29961430.21946356X-RAY DIFFRACTION99
4.6673-5.3420.26211410.22096417X-RAY DIFFRACTION99
5.342-6.72760.24421240.22236476X-RAY DIFFRACTION98
6.7276-49.29220.21451440.21036561X-RAY DIFFRACTION94
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)
10.58930.8654-0.32691.3668-0.19510.26350.0137-0.01570.10780.23430.10330.09450.0801-0.0567-0.07210.33490.15920.01430.4950.08170.4485-19.894542.258434.6998
22.2816-1.53291.1231.36770.23650.99160.06610.38920.09680.107-0.1845-0.1222-0.31140.07580.14770.30070.12740.06040.65380.09080.5818-38.431671.773113.0245
31.5920.54830.26791.11780.3240.173-0.2142-0.11190.1710.03810.14770.0724-0.0228-0.12070.05640.31110.2103-0.05190.6461-0.03950.486610.408323.724255.5134
41.7514-0.77210.94180.9539-0.01610.6567-0.15260.5107-0.122-0.3869-0.09290.2356-0.03680.2250.12240.37970.23120.09060.369-0.02150.311545.197920.999376.7684
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1CHAIN A
2X-RAY DIFFRACTION2CHAIN B
3X-RAY DIFFRACTION3CHAIN C
4X-RAY DIFFRACTION4CHAIN D

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