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1cip
From Proteopedia
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| - | [[Image:1cip.gif|left|200px]] | + | [[Image:1cip.gif|left|200px]] |
| - | + | ||
| - | '''GI-ALPHA-1 SUBUNIT OF GUANINE NUCLEOTIDE-BINDING PROTEIN COMPLEXED WITH A GTP ANALOGUE''' | + | {{Structure |
| + | |PDB= 1cip |SIZE=350|CAPTION= <scene name='initialview01'>1cip</scene>, resolution 1.5Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'>GNP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''GI-ALPHA-1 SUBUNIT OF GUANINE NUCLEOTIDE-BINDING PROTEIN COMPLEXED WITH A GTP ANALOGUE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CIP is a [ | + | 1CIP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CIP OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10358003 10358003] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: gtpase]] | [[Category: gtpase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:24:52 2008'' |
Revision as of 08:24, 20 March 2008
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| , resolution 1.5Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Thu Mar 20 10:24:52 2008
Categories: Rattus norvegicus | Single protein | Coleman, D. | Sprang, S. | GNP | MG | G protein | Gtpase
