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- PDB-4nxv: Crystal structure of the cytosolic domain of human MiD51 -

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Basic information

Entry
Database: PDB / ID: 4nxv
TitleCrystal structure of the cytosolic domain of human MiD51
ComponentsMitochondrial dynamic protein MID51
KeywordsTRANSFERASE / protein-nucleotide complex / nucleotidyltransferase / protein-protein interaction / ADP / GDP / membrane-anchored / mitochondrial fission / mitochondria
Function / homology
Function and homology information


mitochondrial fission / positive regulation of mitochondrial fission / positive regulation of protein targeting to membrane / ADP binding / GDP binding / cellular response to hypoxia / mitochondrial outer membrane / mitochondrion / identical protein binding
Similarity search - Function
Mitochondrial dynamics protein MID49/MID51 / : / Mitochondrial dynamics protein MID51-like, C-terminal domain / Beta Polymerase; domain 2 - #90 / Poly(a)-polymerase, middle domain - #40 / Poly(a)-polymerase, middle domain / Mab-21-like, HhH/H2TH-like domain / Mab-21 protein HhH/H2TH-like domain / Mab-21 protein nucleotidyltransferase domain / Mab-21-like ...Mitochondrial dynamics protein MID49/MID51 / : / Mitochondrial dynamics protein MID51-like, C-terminal domain / Beta Polymerase; domain 2 - #90 / Poly(a)-polymerase, middle domain - #40 / Poly(a)-polymerase, middle domain / Mab-21-like, HhH/H2TH-like domain / Mab-21 protein HhH/H2TH-like domain / Mab-21 protein nucleotidyltransferase domain / Mab-21-like / Mab-21 / Beta Polymerase; domain 2 / 2-Layer Sandwich / Orthogonal Bundle / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-DIPHOSPHATE / Mitochondrial dynamics protein MIEF1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsRichter, V. / Kvansakul, M. / Ryan, M.T.
CitationJournal: J.Cell Biol. / Year: 2014
Title: Structural and functional analysis of MiD51, a dynamin receptor required for mitochondrial fission.
Authors: Richter, V. / Palmer, C.S. / Osellame, L.D. / Singh, A.P. / Elgass, K. / Stroud, D.A. / Sesaki, H. / Kvansakul, M. / Ryan, M.T.
History
DepositionDec 9, 2013Deposition site: RCSB / Processing site: RCSB
Revision 1.0Dec 25, 2013Provider: repository / Type: Initial release
Revision 1.1Mar 19, 2014Group: Database references
Revision 1.2Feb 28, 2024Group: Data collection / Database references / Derived calculations
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Mitochondrial dynamic protein MID51
B: Mitochondrial dynamic protein MID51
C: Mitochondrial dynamic protein MID51
D: Mitochondrial dynamic protein MID51
hetero molecules


Theoretical massNumber of molelcules
Total (without water)157,54013
Polymers155,2914
Non-polymers2,2499
Water6,413356
1
A: Mitochondrial dynamic protein MID51
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,3623
Polymers38,8231
Non-polymers5392
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Mitochondrial dynamic protein MID51
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,5545
Polymers38,8231
Non-polymers7314
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Mitochondrial dynamic protein MID51
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,3583
Polymers38,8231
Non-polymers5352
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Mitochondrial dynamic protein MID51
hetero molecules


Theoretical massNumber of molelcules
Total (without water)39,2662
Polymers38,8231
Non-polymers4431
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
A: Mitochondrial dynamic protein MID51
hetero molecules

D: Mitochondrial dynamic protein MID51
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,6285
Polymers77,6452
Non-polymers9823
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_546x,y-1,z+11
Buried area4100 Å2
ΔGint-46 kcal/mol
Surface area29720 Å2
MethodPISA
6
B: Mitochondrial dynamic protein MID51
hetero molecules

C: Mitochondrial dynamic protein MID51
hetero molecules


Theoretical massNumber of molelcules
Total (without water)78,9128
Polymers77,6452
Non-polymers1,2676
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_554x,y,z-11
Buried area4340 Å2
ΔGint-47 kcal/mol
Surface area30080 Å2
MethodPISA
Unit cell
Length a, b, c (Å)72.343, 79.093, 80.052
Angle α, β, γ (deg.)65.81, 84.36, 64.08
Int Tables number1
Space group name H-MP1

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Components

#1: Protein
Mitochondrial dynamic protein MID51 / Mitochondrial dynamic protein of 51 kDa / Mitochondrial elongation factor 1 / Smith-Magenis ...Mitochondrial dynamic protein of 51 kDa / Mitochondrial elongation factor 1 / Smith-Magenis syndrome chromosomal region candidate gene 7 protein-like


Mass: 38822.656 Da / Num. of mol.: 4 / Fragment: unp residues 119-463
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human)
Gene: candidate 7-like, MID51, MIEF1, SMCR7L, Smith-Magenis syndrome chromosome region
Plasmid: pGEX-4T-1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: Q9NQG6
#2: Chemical
ChemComp-GDP / GUANOSINE-5'-DIPHOSPHATE / Guanosine diphosphate


Type: RNA linking / Mass: 443.201 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H15N5O11P2 / Comment: GDP, energy-carrying molecule*YM
#3: Chemical
ChemComp-SO4 / SULFATE ION / Sulfate


Mass: 96.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: SO4
#4: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL / Glycerol


Mass: 92.094 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C3H8O3
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 356 / Source method: isolated from a natural source / Formula: H2O

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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: 2.41 Å3/Da / Density % sol: 48.92 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 16% PEG 8000, 0.1M HEPES, 10% 2-propanol, 0.2M ammonium sulfate, 0.01M GDP, 0.02M manganese chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Aug 23, 2013
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 2.3→40 Å / Num. obs: 63108 / % possible obs: 98.1 % / Redundancy: 2.5 % / Biso Wilson estimate: 27.4 Å2 / Rmerge(I) obs: 0.078 / Net I/σ(I): 9.4
Reflection shellResolution: 2.3→2.42 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.447 / Mean I/σ(I) obs: 2.2 / Num. unique all: 63108

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
PHENIXmodel building
PHENIX(phenix.refine: 1.8.2_1309)refinement
XDSdata reduction
SCALAdata scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.3→39.046 Å / SU ML: 0.28 / σ(F): 1.97 / Phase error: 25.72 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2375 3169 5.02 %random
Rwork0.1913 ---
obs-63108 98.1 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.3→39.046 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10363 0 138 356 10857
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00510754
X-RAY DIFFRACTIONf_angle_d0.90314703
X-RAY DIFFRACTIONf_dihedral_angle_d14.9283965
X-RAY DIFFRACTIONf_chiral_restr0.051695
X-RAY DIFFRACTIONf_plane_restr0.0041870
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.3-2.33430.33511340.28182610X-RAY DIFFRACTION97
2.3343-2.37080.35371260.26162583X-RAY DIFFRACTION98
2.3708-2.40970.31161440.25542602X-RAY DIFFRACTION97
2.4097-2.45120.29641240.24442588X-RAY DIFFRACTION98
2.4512-2.49580.29061470.23212642X-RAY DIFFRACTION98
2.4958-2.54380.29391380.23292567X-RAY DIFFRACTION98
2.5438-2.59570.29511580.22042588X-RAY DIFFRACTION99
2.5957-2.65210.25981310.21472579X-RAY DIFFRACTION98
2.6521-2.71380.26641310.21212639X-RAY DIFFRACTION98
2.7138-2.78160.24871280.21772642X-RAY DIFFRACTION98
2.7816-2.85680.24551250.2122607X-RAY DIFFRACTION98
2.8568-2.94090.27211420.21542584X-RAY DIFFRACTION98
2.9409-3.03580.29951430.20512615X-RAY DIFFRACTION98
3.0358-3.14420.28121360.21262629X-RAY DIFFRACTION99
3.1442-3.270.27191530.19712581X-RAY DIFFRACTION98
3.27-3.41880.22671410.18752625X-RAY DIFFRACTION98
3.4188-3.59890.21521320.18422624X-RAY DIFFRACTION98
3.5989-3.82420.23371470.17732589X-RAY DIFFRACTION98
3.8242-4.11920.19241280.15962607X-RAY DIFFRACTION98
4.1192-4.53320.19571210.14732644X-RAY DIFFRACTION99
4.5332-5.18780.18231580.15332578X-RAY DIFFRACTION98
5.1878-6.53110.24991440.19032589X-RAY DIFFRACTION98
6.5311-39.05130.16621380.16292627X-RAY DIFFRACTION99
Refinement TLS params.

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

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
18.58980.434-2.53921.2929-0.4063.49470.6660.45011.45020.0386-0.17480.4821-0.7622-0.1457-0.530.40070.02050.08410.3254-0.01050.54091.2582-9.7803-16.8523
23.9399-1.0032-0.32482.3409-0.88792.8415-0.0978-0.97430.00870.50330.26390.4365-0.2134-0.3894-0.25980.28240.03160.02850.631-0.03710.3018-15.3714-29.2532-1.09
31.2471-1.01080.32343.4578-0.75191.45550.0089-0.2299-0.5046-0.14030.44030.4166-0.0054-0.4658-0.40310.2947-0.0262-0.03020.45570.13580.4156-7.9231-52.4938-0.8723
43.2951-1.68420.77634.6284-0.87250.349-0.0776-0.12830.0073-0.55270.39721.07660.2053-0.7813-0.2770.42540.0028-0.01990.72190.13950.6224-26.8193-31.4836-7.0071
55.5721-3.2991.27224.4936-0.57181.4277-0.1610.02350.1275-0.31750.042-0.0562-0.3164-0.4530.17230.3561-0.046-0.02920.36560.04950.2259-11.4432-34.9043-9.199
61.55661.4622-0.24782.7225-1.28861.05960.1781-0.20210.21690.2398-0.16230.1454-0.11310.0439-0.06310.22930.02430.05020.3055-0.0480.29732.0792-26.9227-8.998
72.38461.8971-0.08334.0421-0.54761.52630.0579-0.0862-0.06430.0622-0.1159-0.32940.07310.23640.09180.1807-0.00320.03390.2407-0.0020.24811.5208-27.039-12.2813
83.32010.4298-0.75230.1493-0.34361.9921-0.27850.49880.1306-0.69890.36550.13910.2276-0.16020.03650.2978-0.02720.00280.34690.01960.27776.7792-25.1253-27.5513
91.5969-0.36990.08121.55230.66221.58540.14310.1158-0.08140.04080.1922-0.54960.02380.3162-0.39250.2648-0.00770.01210.36330.02020.321-25.264-8.3097-30.0973
102.06491.2661-0.80841.41621.00792.1342-0.0082-0.0346-0.26940.1481-0.018-0.07560.13410.11470.030.2670.0172-0.01640.2430.0440.2273-45.1967-22.6651-35.0212
114.841-1.83266.89833.0294-0.62872.16450.544-0.9201-0.6980.4157-0.276-0.1330.5663-0.1961-0.59030.4122-0.0221-0.11580.61090.02970.4259-21.7096-20.5108-23.5433
121.31290.74430.45274.08691.19440.64560.0704-0.14360.13440.188-0.093-0.0037-0.05190.03050.03510.2515-0.0252-0.00050.27420.0080.1877-39.17660.8202-22.8782
133.2435-2.3754-0.6482.70170.78930.5690.1007-0.16720.1221-0.0447-0.0238-0.4830.2477-0.0136-0.14620.2277-0.0262-0.01240.3132-0.0010.485211.10885.63397.0076
143.36660.2532-0.89650.6538-0.15491.09090.03730.0266-0.14790.0199-0.0066-0.09880.0410.1109-0.04940.18560.0206-0.01720.23030.00360.1732-22.49859.032617.2416
153.087-0.154-1.25330.64290.02942.7615-0.14150.2591-0.23110.19990.07550.04320.1515-0.21080.03340.1820.0107-0.01980.23350.00080.2745-42.12631.970416.2274
166.13265.31230.19669.51370.24310.8565-0.43290.79280.5628-0.75880.59950.0828-0.3825-0.0036-0.18930.3014-0.0128-0.03160.37320.06010.3906-26.168721.698911.4446
174.37120.2997-1.33542.18010.25371.2718-0.02160.2842-0.1049-0.07220.0051-0.1067-0.10360.1-0.01290.2597-0.0205-0.02720.3075-0.01750.1939-13.0975.451110.6582
186.42461.4667-0.11752.83570.91691.8976-0.08750.5846-0.8766-0.33660.0818-0.52550.02660.18860.06330.29670.00890.07130.3609-0.09680.5126-2.4859-5.12293.4394
192.18221.0983-0.18020.7809-0.22262.36650.01930.34560.3282-0.24660.1362-0.1564-0.4449-0.0281-0.1360.40650.00050.00010.32620.0370.32563.970415.0033-50.9315
201.2859-2.6746-0.8326.54772.01532.3658-0.059-0.2291-0.04770.56480.06880.02160.13850.08960.00690.31160.0194-0.01490.2626-0.01940.28828.3616-13.3254-51
217.8417-0.86182.10175.63651.66491.1960.4631-0.5537-0.12080.6226-0.2372-1.0183-0.76041.0205-0.25030.5266-0.15830.02850.6266-0.13460.665920.584212.356-48.3115
222.9462-0.2849-1.75922.81080.95653.14280.00620.31450.19830.1345-0.04290.3197-0.2667-0.33880.01210.32420.0398-0.00820.30320.0250.2365-7.41057.499-43.9307
230.1329-0.1943-0.11132.60790.5440.2382-0.0645-0.49780.20680.63290.22380.4919-0.199-0.20530.10420.6275-0.02910.10670.667-0.00150.5381-13.08313.3082-27.6976
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 132 through 150 )
2X-RAY DIFFRACTION2chain 'A' and (resid 151 through 208 )
3X-RAY DIFFRACTION3chain 'A' and (resid 209 through 271 )
4X-RAY DIFFRACTION4chain 'A' and (resid 272 through 296 )
5X-RAY DIFFRACTION5chain 'A' and (resid 297 through 333 )
6X-RAY DIFFRACTION6chain 'A' and (resid 334 through 381 )
7X-RAY DIFFRACTION7chain 'A' and (resid 382 through 439 )
8X-RAY DIFFRACTION8chain 'A' and (resid 440 through 462 )
9X-RAY DIFFRACTION9chain 'B' and (resid 132 through 200 )
10X-RAY DIFFRACTION10chain 'B' and (resid 201 through 283 )
11X-RAY DIFFRACTION11chain 'B' and (resid 284 through 305 )
12X-RAY DIFFRACTION12chain 'B' and (resid 306 through 462 )
13X-RAY DIFFRACTION13chain 'C' and (resid 126 through 150 )
14X-RAY DIFFRACTION14chain 'C' and (resid 151 through 235 )
15X-RAY DIFFRACTION15chain 'C' and (resid 236 through 258 )
16X-RAY DIFFRACTION16chain 'C' and (resid 259 through 296 )
17X-RAY DIFFRACTION17chain 'C' and (resid 297 through 381 )
18X-RAY DIFFRACTION18chain 'C' and (resid 382 through 462 )
19X-RAY DIFFRACTION19chain 'D' and (resid 132 through 207 )
20X-RAY DIFFRACTION20chain 'D' and (resid 208 through 273 )
21X-RAY DIFFRACTION21chain 'D' and (resid 274 through 296 )
22X-RAY DIFFRACTION22chain 'D' and (resid 297 through 439 )
23X-RAY DIFFRACTION23chain 'D' and (resid 440 through 462 )

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