1fkm
From Proteopedia
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| - | [[Image:1fkm.gif|left|200px]]<br /><applet load="1fkm" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1fkm, resolution 1.90Å" /> | ||
| - | '''CRYSTAL STRUCTURE OF THE YPT/RAB-GAP DOMAIN OF GYP1P'''<br /> | ||
| - | == | + | ==CRYSTAL STRUCTURE OF THE YPT/RAB-GAP DOMAIN OF GYP1P== |
| + | <StructureSection load='1fkm' size='340' side='right'caption='[[1fkm]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1fkm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FKM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FKM FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fkm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fkm OCA], [https://pdbe.org/1fkm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fkm RCSB], [https://www.ebi.ac.uk/pdbsum/1fkm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fkm ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/GYP1_YEAST GYP1_YEAST] Stimulates specifically the GTPase activity of YPT1. Functions on the Golgi as a negative regulator of YPT1.<ref>PMID:11359917</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fk/1fkm_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fkm ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
We present the 1.9 A resolution crystal structure of the catalytic domain of Gyp1p, a specific GTPase activating protein (GAP) for Ypt proteins, the yeast homologues of Rab proteins, which are involved in vesicular transport. Gyp1p is a member of a large family of eukaryotic proteins with shared sequence motifs. Previously, no structural information was available for any member of this class of proteins. The GAP domain of Gyp1p was found to be fully alpha-helical. However, the observed fold does not superimpose with other alpha-helical GAPs (e.g. Ras- and Cdc42/Rho-GAP). The conserved and catalytically crucial arginine residue, identified by mutational analysis, is in a comparable position to the arginine finger in the Ras- and Cdc42-GAPs, suggesting that Gyp1p utilizes an arginine finger in the GAP reaction, in analogy to Ras- and Cdc42-GAPs. A model for the interaction between Gyp1p and the Ypt protein satisfying biochemical data is given. | We present the 1.9 A resolution crystal structure of the catalytic domain of Gyp1p, a specific GTPase activating protein (GAP) for Ypt proteins, the yeast homologues of Rab proteins, which are involved in vesicular transport. Gyp1p is a member of a large family of eukaryotic proteins with shared sequence motifs. Previously, no structural information was available for any member of this class of proteins. The GAP domain of Gyp1p was found to be fully alpha-helical. However, the observed fold does not superimpose with other alpha-helical GAPs (e.g. Ras- and Cdc42/Rho-GAP). The conserved and catalytically crucial arginine residue, identified by mutational analysis, is in a comparable position to the arginine finger in the Ras- and Cdc42-GAPs, suggesting that Gyp1p utilizes an arginine finger in the GAP reaction, in analogy to Ras- and Cdc42-GAPs. A model for the interaction between Gyp1p and the Ypt protein satisfying biochemical data is given. | ||
| - | + | Crystal structure of the GAP domain of Gyp1p: first insights into interaction with Ypt/Rab proteins.,Rak A, Fedorov R, Alexandrov K, Albert S, Goody RS, Gallwitz D, Scheidig AJ EMBO J. 2000 Oct 2;19(19):5105-13. PMID:11013213<ref>PMID:11013213</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1fkm" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | + | [[Category: Albert S]] | |
| - | [[Category: Albert | + | [[Category: Alexandrov K]] |
| - | [[Category: Alexandrov | + | [[Category: Fedorov R]] |
| - | [[Category: Fedorov | + | [[Category: Gallwitz D]] |
| - | [[Category: Gallwitz | + | [[Category: Goody RS]] |
| - | [[Category: Goody | + | [[Category: Rak A]] |
| - | [[Category: Rak | + | [[Category: Scheidig AJ]] |
| - | [[Category: Scheidig | + | |
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Current revision
CRYSTAL STRUCTURE OF THE YPT/RAB-GAP DOMAIN OF GYP1P
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