1gia
From Proteopedia
(New page: 200px<br /> <applet load="1gia" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gia, resolution 2.0Å" /> '''STRUCTURE OF ACTIVE ...) |
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caption="1gia, resolution 2.0Å" /> | caption="1gia, resolution 2.0Å" /> | ||
'''STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS'''<br /> | '''STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1GIA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with MG and GSP as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1GIA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb58_1.html G Proteins]]. Full crystallographic information is available from [http:// | + | 1GIA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GSP:'>GSP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1GIA with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb58_1.html G Proteins]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GIA OCA]. |
==Reference== | ==Reference== | ||
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[[Category: signal transduction protein]] | [[Category: signal transduction protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:53:44 2008'' |
Revision as of 13:53, 15 February 2008
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STRUCTURE OF ACTIVE CONFORMATIONS OF GIA1 AND THE MECHANISM OF GTP HYDROLYSIS
Overview
Mechanisms of guanosine triphosphate (GTP) hydrolysis by members of the G, protein alpha subunit-p21ras superfamily of guanosine triphosphatases have, been studied extensively but have not been well understood., High-resolution x-ray structures of the GTP gamma S and GDP.AlF4-, complexes formed by the G protein Gi alpha 1 demonstrate specific roles in, transition-state stabilization for two highly conserved residues., Glutamine204 (Gln61 in p21ras) stabilizes and orients the hydrolytic water, in the trigonal-bipyramidal transition state. Arginine 178 stabilizes the, negative charge at the equatorial oxygen atoms of the pentacoordinate, phosphate intermediate. Conserved only in the G alpha family, this residue, may account for the higher hydrolytic rate of G alpha proteins relative to, those of the p21ras family members. The fold of Gi alpha 1 differs from, that of the homologous Gt alpha subunit in the conformation of a, helix-loop sequence located in the alpha-helical domain that is, characteristic of these proteins; this site may participate in effector, binding. The amino-terminal 33 residues are disordered in GTP gamma S-Gi, alpha 1, suggesting a mechanism that may promote release of the beta gamma, subunit complex when the alpha subunit is activated by GTP.
About this Structure
1GIA is a Single protein structure of sequence from Rattus norvegicus with and as ligands. The following page contains interesting information on the relation of 1GIA with [G Proteins]. Full crystallographic information is available from OCA.
Reference
Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis., Coleman DE, Berghuis AM, Lee E, Linder ME, Gilman AG, Sprang SR, Science. 1994 Sep 2;265(5177):1405-12. PMID:8073283
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