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- PDB-1huq: 1.8A CRYSTAL STRUCTURE OF THE MONOMERIC GTPASE RAB5C (MOUSE) -

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Basic information

Entry
Database: PDB / ID: 1huq
Title1.8A CRYSTAL STRUCTURE OF THE MONOMERIC GTPASE RAB5C (MOUSE)
ComponentsRAB5C
KeywordsPROTEIN TRANSPORT / G-protein / GTP hydrolysis / endocytosis / Rab protein / membrane trafficking
Function / homology
Function and homology information


RAB geranylgeranylation / RAB GEFs exchange GTP for GDP on RABs / : / plasma membrane to endosome transport / Golgi Associated Vesicle Biogenesis / endosome organization / Clathrin-mediated endocytosis / regulation of endocytosis / endocytic vesicle / lipid droplet ...RAB geranylgeranylation / RAB GEFs exchange GTP for GDP on RABs / : / plasma membrane to endosome transport / Golgi Associated Vesicle Biogenesis / endosome organization / Clathrin-mediated endocytosis / regulation of endocytosis / endocytic vesicle / lipid droplet / G protein activity / small monomeric GTPase / Neutrophil degranulation / intracellular protein transport / GDP binding / melanosome / endocytosis / early endosome membrane / cytoplasmic vesicle / early endosome / endosome / GTPase activity / GTP binding / plasma membrane
Similarity search - Function
small GTPase Rab1 family profile. / Rho (Ras homology) subfamily of Ras-like small GTPases / Small GTPase / Ras family / Small GTP-binding protein domain / P-loop containing nucleotide triphosphate hydrolases / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / Ras-related protein Rab-5C
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.8 Å
AuthorsMerithew, E. / Hatherly, S. / Dumas, J.J. / Lawe, D.C. / Heller-Harrison, R. / Lambright, D.G.
CitationJournal: J.Biol.Chem. / Year: 2001
Title: Structural plasticity of an invariant hydrophobic triad in the switch regions of Rab GTPases is a determinant of effector recognition.
Authors: Merithew, E. / Hatherly, S. / Dumas, J.J. / Lawe, D.C. / Heller-Harrison, R. / Lambright, D.G.
History
DepositionJan 4, 2001Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 7, 2001Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: RAB5C
hetero molecules


Theoretical massNumber of molelcules
Total (without water)18,8203
Polymers18,2741
Non-polymers5472
Water2,756153
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)35.850, 64.000, 65.914
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

#1: Protein RAB5C


Mass: 18273.828 Da / Num. of mol.: 1 / Fragment: GTPASE DOMAIN
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Escherichia coli (E. coli) / References: UniProt: P35278
#2: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Mg
#3: Chemical ChemComp-GNP / PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER / 5'-Guanylyl imidodiphosphate


Mass: 522.196 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C10H17N6O13P3
Comment: GppNHp, GMPPNP, energy-carrying molecule analogue*YM
#4: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 153 / 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: 2.07 Å3/Da / Density % sol: 40.54 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6
Details: PEG-6000, sodium chloride, magnesium chloride, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K
Crystal
*PLUS
Density % sol: 35 %
Crystal grow
*PLUS
Temperature: 4 ℃
Components of the solutions
*PLUS
IDConc.Common nameCrystal-IDSol-IDChemical formula
110 %PEG60001reservoir
250 mMMES1reservoir
30.2 M1reservoirNaCl
40.5 mM1reservoirMgCl2

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 Å
DetectorType: MARRESEARCH / Detector: IMAGE PLATE / Date: Aug 15, 2000 / Details: MIRRORS
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.5418 Å / Relative weight: 1
ReflectionResolution: 1.8→20 Å / Num. all: 14494 / Num. obs: 14494 / % possible obs: 98.8 % / Observed criterion σ(I): -3 / Redundancy: 4 % / Biso Wilson estimate: 15.5 Å2 / Rsym value: 0.054 / Net I/σ(I): 20.3
Reflection shellResolution: 1.8→1.85 Å / Redundancy: 4 % / Mean I/σ(I) obs: 5.4 / Num. unique all: 1125 / Rsym value: 0.227 / % possible all: 94.9
Reflection
*PLUS
Rmerge(I) obs: 0.054
Reflection shell
*PLUS
% possible obs: 94.9 % / Rmerge(I) obs: 0.227

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Processing

Software
NameVersionClassification
AMoREphasing
X-PLOR3.1refinement
DENZOdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3RAB
Resolution: 1.8→20 Å / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.232 679 -Random
Rwork0.195 ---
all-14460 --
obs-13580 94 %-
Refinement stepCycle: LAST / Resolution: 1.8→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1285 0 33 153 1471
Software
*PLUS
Name: X-PLOR / Version: 3.1 / Classification: refinement
Refine LS restraints
*PLUS
Refine-IDTypeDev ideal
X-RAY DIFFRACTIONx_bond_d0.006
X-RAY DIFFRACTIONx_angle_d
X-RAY DIFFRACTIONx_angle_deg1.2
X-RAY DIFFRACTIONx_dihedral_angle_d
X-RAY DIFFRACTIONx_improper_angle_d
X-RAY DIFFRACTIONx_mcbond_it
X-RAY DIFFRACTIONx_scbond_it
X-RAY DIFFRACTIONx_mcangle_it
X-RAY DIFFRACTIONx_scangle_it

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