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- PDB-2i59: Solution structure of RGS10 -

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Basic information

Entry
Database: PDB / ID: 2i59
TitleSolution structure of RGS10
ComponentsRegulator of G-protein signaling 10
KeywordsSIGNALING PROTEIN / Regulator of G-protein signaling / Structural Genomics / Structural Genomics Consortium / SGC
Function / homology
Function and homology information


regulation of G protein-coupled receptor signaling pathway / positive regulation of GTPase activity / G-protein alpha-subunit binding / negative regulation of signal transduction / GTPase activator activity / G protein-coupled acetylcholine receptor signaling pathway / G alpha (i) signalling events / nuclear body / G protein-coupled receptor signaling pathway / GTPase activity ...regulation of G protein-coupled receptor signaling pathway / positive regulation of GTPase activity / G-protein alpha-subunit binding / negative regulation of signal transduction / GTPase activator activity / G protein-coupled acetylcholine receptor signaling pathway / G alpha (i) signalling events / nuclear body / G protein-coupled receptor signaling pathway / GTPase activity / synapse / nucleoplasm / nucleus / plasma membrane / cytosol
Similarity search - Function
RGS10, RGS domain / : / RGS, subdomain 1/3 / Regulator of G-protein Signalling 4, domain 2 / Regulator of G-protein Signalling 4; domain 2 / Regulator of G protein signaling domain / RGS domain / RGS domain profile. / Regulator of G protein signalling domain / RGS, subdomain 2 ...RGS10, RGS domain / : / RGS, subdomain 1/3 / Regulator of G-protein Signalling 4, domain 2 / Regulator of G-protein Signalling 4; domain 2 / Regulator of G protein signaling domain / RGS domain / RGS domain profile. / Regulator of G protein signalling domain / RGS, subdomain 2 / RGS domain superfamily / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Regulator of G-protein signaling 10
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsFedorov, O. / Higman, V.A. / Diehl, A. / Leidert, M. / Lemak, A. / Schmieder, P. / Oschkinat, H. / Elkins, J. / Soundarajan, M. / Doyle, D.A. ...Fedorov, O. / Higman, V.A. / Diehl, A. / Leidert, M. / Lemak, A. / Schmieder, P. / Oschkinat, H. / Elkins, J. / Soundarajan, M. / Doyle, D.A. / Arrowsmith, C. / Sundstrom, M. / Weigelt, J. / Edwards, A. / Ball, L.J. / Structural Genomics Consortium (SGC)
CitationJournal: Proc.Natl.Acad.Sci.Usa / Year: 2008
Title: Structural diversity in the RGS domain and its interaction with heterotrimeric G protein alpha-subunits.
Authors: Soundararajan, M. / Willard, F.S. / Kimple, A.J. / Turnbull, A.P. / Ball, L.J. / Schoch, G.A. / Gileadi, C. / Fedorov, O.Y. / Dowler, E.F. / Higman, V.A. / Hutsell, S.Q. / Sundstrom, M. / ...Authors: Soundararajan, M. / Willard, F.S. / Kimple, A.J. / Turnbull, A.P. / Ball, L.J. / Schoch, G.A. / Gileadi, C. / Fedorov, O.Y. / Dowler, E.F. / Higman, V.A. / Hutsell, S.Q. / Sundstrom, M. / Doyle, D.A. / Siderovski, D.P.
History
DepositionAug 24, 2006Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 31, 2006Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 19, 2020Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _pdbx_database_status.status_code_cs / _struct_ref_seq_dif.details
Revision 1.4Jun 14, 2023Group: Database references / Other / Category: database_2 / pdbx_database_status
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.status_code_nmr_data
Revision 1.5May 8, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2 / Item: _database_2.pdbx_DOI

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Regulator of G-protein signaling 10


Theoretical massNumber of molelcules
Total (without water)16,5111
Polymers16,5111
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein Regulator of G-protein signaling 10 / RGS10


Mass: 16510.805 Da / Num. of mol.: 1 / Fragment: Regulator of G-protein signaling domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RGS10 / Production host: Escherichia coli (E. coli) / References: UniProt: O43665

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Experimental details

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Experiment

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

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Sample preparation

DetailsContents: U-15N, 13C RGS10, 20 mM Phosphate, 50 mM NaCl, 90% H2O, 10% D2O
Solvent system: 90% H2O/10% D2O
Sample conditionsIonic strength: 50 mM NaCl, 20 mM phosphate / pH: 7 / Pressure: ambient / Temperature: 298 K

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DMXBrukerDMX7501
Bruker DMXBrukerDMX6002

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Processing

NMR software
NameVersionDeveloperClassification
CNS1BRUNGERrefinement
CYANA2.1Guntertstructure solution
XPLOR-NIH2.14BRUNGERstructure solution
RefinementMethod: simulated annealing / Software ordinal: 1
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 20

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