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- PDB-2dky: Solution structure of the SAM-domain of Rho-GTPase-activating pro... -

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Basic information

Entry
Database: PDB / ID: 2dky
TitleSolution structure of the SAM-domain of Rho-GTPase-activating protein 7
ComponentsRho-GTPase-activating protein 7
KeywordsSIGNALING PROTEIN / CELL-FREE PROTEIN SYNTHESIS / PROTEIN REGULATION / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI
Function / homology
Function and homology information


hindbrain morphogenesis / negative regulation of focal adhesion assembly / regulation of Rho protein signal transduction / focal adhesion assembly / regulation of small GTPase mediated signal transduction / negative regulation of stress fiber assembly / negative regulation of Rho protein signal transduction / RHOB GTPase cycle / cortical actin cytoskeleton / RHOC GTPase cycle ...hindbrain morphogenesis / negative regulation of focal adhesion assembly / regulation of Rho protein signal transduction / focal adhesion assembly / regulation of small GTPase mediated signal transduction / negative regulation of stress fiber assembly / negative regulation of Rho protein signal transduction / RHOB GTPase cycle / cortical actin cytoskeleton / RHOC GTPase cycle / positive regulation of execution phase of apoptosis / RHOQ GTPase cycle / CDC42 GTPase cycle / RHOA GTPase cycle / heart morphogenesis / positive regulation of protein dephosphorylation / forebrain development / RAC1 GTPase cycle / SH2 domain binding / negative regulation of cell migration / GTPase activator activity / caveola / neural tube closure / regulation of actin cytoskeleton organization / ruffle membrane / activation of cysteine-type endopeptidase activity involved in apoptotic process / regulation of cell shape / actin cytoskeleton organization / membrane raft / negative regulation of cell population proliferation / intracellular membrane-bounded organelle / focal adhesion / lipid binding / apoptotic process / endoplasmic reticulum / signal transduction / nucleus / cytoplasm / cytosol
Similarity search - Function
Helix Hairpins - #2070 / in StAR and phosphatidylcholine transfer protein / START domain / START domain / START domain profile. / Rho GTPase-activating protein domain / RhoGAP domain / Rho GTPase-activating proteins domain profile. / GTPase-activator protein for Rho-like GTPases / Rho GTPase activation protein ...Helix Hairpins - #2070 / in StAR and phosphatidylcholine transfer protein / START domain / START domain / START domain profile. / Rho GTPase-activating protein domain / RhoGAP domain / Rho GTPase-activating proteins domain profile. / GTPase-activator protein for Rho-like GTPases / Rho GTPase activation protein / START-like domain superfamily / SAM domain (Sterile alpha motif) / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Helix Hairpins / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Rho GTPase-activating protein 7
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsGoroncy, A.K. / Sato, M. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI)
CitationJournal: To be Published
Title: Solution structure of the SAM-domain of Rho-GTPase-activating protein 7
Authors: Goroncy, A.K. / Sato, M. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S.
History
DepositionApr 14, 2006Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Apr 24, 2007Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 9, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.4May 29, 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: Rho-GTPase-activating protein 7


Theoretical massNumber of molelcules
Total (without water)10,2001
Polymers10,2001
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100structures with the least restraint violations
RepresentativeModel #1fewest violations

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Components

#1: Protein Rho-GTPase-activating protein 7 / Rho-type GTPase-activating protein 7 / Deleted in liver cancer 1 protein / Dlc-1 / HP protein / ...Rho-type GTPase-activating protein 7 / Deleted in liver cancer 1 protein / Dlc-1 / HP protein / StAR-related lipid transfer protein 12 / StARD12 / START domain-containing protein 12


Mass: 10199.683 Da / Num. of mol.: 1 / Fragment: SAM-domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Description: CELL-FREE PROTEIN SYNTHESIS / Gene: DLC1, ARHGAP7, KIAA1723, STARD12 / Plasmid: P050207-01 / References: UniProt: Q96QB1

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
1213D 13C-separated NOESY

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Sample preparation

DetailsContents: 1.08mM SAM DOMAIN, 20mM d-TRIS-HCL, 100mM NaCl, 1mM d-DTT, 0.02% NaN3, 90% H2O, 10% D2O
Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 120mM / pH: 7.0 / Pressure: AMBIENT / Temperature: 296 K

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NMR measurement

NMR spectrometerType: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz

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Processing

NMR software
NameVersionDeveloperClassification
CYANA2.0.17P.GUNTERT ET AL.refinement
CYANA2.0.17P.GUNTERT ET AL.structure solution
XwinNMR3.5BRUKERcollection
NMRPipe20031121FRANK DELAGLIOprocessing
NMRView5.0.4BRUCE A. JOHNSONdata analysis
KUJIRA0.899aNAOHIRO KOBAYASHIdata analysis
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: fewest violations
NMR ensembleConformer selection criteria: structures with the least restraint violations
Conformers calculated total number: 100 / Conformers submitted total number: 20

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