1gwn: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1gwn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GWN FirstGlance]. <br> | <table><tr><td colspan='2'>[[1gwn]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GWN FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GTP:GUANOSINE-5-TRIPHOSPHATE'>GTP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gwn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gwn RCSB], [http://www.ebi.ac.uk/pdbsum/1gwn PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gwn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1gwn RCSB], [http://www.ebi.ac.uk/pdbsum/1gwn PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Garavini, H | [[Category: Garavini, H]] | ||
[[Category: Keep, N H | [[Category: Keep, N H]] | ||
[[Category: Mcalister, M S.B | [[Category: Mcalister, M S.B]] | ||
[[Category: Phelan, J P | [[Category: Phelan, J P]] | ||
[[Category: Ridley, A J | [[Category: Ridley, A J]] | ||
[[Category: Riento, K | [[Category: Riento, K]] | ||
[[Category: Gtpase]] | [[Category: Gtpase]] | ||
[[Category: Inactive gtpase]] | [[Category: Inactive gtpase]] | ||
[[Category: Signal transduction]] | [[Category: Signal transduction]] | ||
Revision as of 03:22, 23 December 2014
THE CRYSTAL STRUCTURE OF THE CORE DOMAIN OF RHOE/RND3 - A CONSTITUTIVELY ACTIVATED SMALL G PROTEINTHE CRYSTAL STRUCTURE OF THE CORE DOMAIN OF RHOE/RND3 - A CONSTITUTIVELY ACTIVATED SMALL G PROTEIN
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe report the 2.1 A crystal structure of the core G protein domain of the unusual Rho family member RhoE/Rnd3 in complex with endogenous GTP and magnesium. Unlike other small G proteins, RhoE, along with two other proteins Rnd1/Rho6 and Rnd2/RhoN, does not hydrolyze GTP. The main reason for this is the presence of serines in the positions equivalent to Ala59 and Gln61 in Ras. The structure shows that there are still water molecules in similar positions to the waters thought to be involved in the hydrolysis reaction in other G proteins. The structure suggests three not necessarily exclusive explanations for the lack of hydrolysis. The lack of the conserved glutamine raises the energy of the transition state inhibiting hydrolysis. The serines may restrain the waters from moving closer to the GTP, a step that is required to attain the transition state. They also stabilize the GTP-bound conformation of switch II and could prevent conformational changes required during hydrolysis. By superposition of the RhoE structure on structures of Rho family proteins in complex with binding partners, we make predictions on RhoE interactions with these partners. Crystal structure of the core domain of RhoE/Rnd3: a constitutively activated small G protein.,Garavini H, Riento K, Phelan JP, McAlister MS, Ridley AJ, Keep NH Biochemistry. 2002 May 21;41(20):6303-10. PMID:12009891[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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