1cip: Difference between revisions

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[[Image:1cip.gif|left|200px]]
[[Image:1cip.gif|left|200px]]


{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cip OCA], [http://www.ebi.ac.uk/pdbsum/1cip PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1cip RCSB]</span>
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'''GI-ALPHA-1 SUBUNIT OF GUANINE NUCLEOTIDE-BINDING PROTEIN COMPLEXED WITH A GTP ANALOGUE'''
'''GI-ALPHA-1 SUBUNIT OF GUANINE NUCLEOTIDE-BINDING PROTEIN COMPLEXED WITH A GTP ANALOGUE'''
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[[Category: Coleman, D.]]
[[Category: Coleman, D.]]
[[Category: Sprang, S.]]
[[Category: Sprang, S.]]
[[Category: g protein]]
[[Category: G protein]]
[[Category: gtpase]]
[[Category: Gtpase]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:22:27 2008''

Revision as of 09:46, 2 May 2008

File:1cip.gif

Template:STRUCTURE 1cip

GI-ALPHA-1 SUBUNIT OF GUANINE NUCLEOTIDE-BINDING PROTEIN COMPLEXED WITH A GTP ANALOGUE


Overview

The structure of the G protein Gialpha1 complexed with the nonhydrolyzable GTP analog guanosine-5'-(betagamma-imino)triphosphate (GppNHp) has been determined at a resolution of 1.5 A. In the active site of Gialpha1. GppNHp, a water molecule is hydrogen bonded to the side chain of Glu43 and to an oxygen atom of the gamma-phosphate group. The side chain of the essential catalytic residue Gln204 assumes a conformation which is distinctly different from that observed in complexes with either guanosine 5'-O-3-thiotriphosphate or the transition state analog GDP.AlF4-. Hydrogen bonding and steric interactions position Gln204 such that it interacts with a presumptive nucleophilic water molecule, but cannot interact with the pentacoordinate transition state. Gln204 must be released from this auto-inhibited state to participate in catalysis. RGS proteins may accelerate the rate of GTP hydrolysis by G protein alpha subunits, in part, by inserting an amino acid side chain into the site occupied by Gln204, thereby destabilizing the auto-inhibited state of Galpha.

About this Structure

1CIP is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

Structure of Gialpha1.GppNHp, autoinhibition in a galpha protein-substrate complex., Coleman DE, Sprang SR, J Biol Chem. 1999 Jun 11;274(24):16669-72. PMID:10358003 Page seeded by OCA on Fri May 2 12:46:27 2008

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