1ek0: Difference between revisions

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-{{Seed}}
-[[Image:1ek0.png|left|200px]]
-<!--
+==GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION==
-The line below this paragraph, containing "STRUCTURE_1ek0", creates the "Structure Box" on the page.
+<StructureSection load='1ek0' size='340' side='right'caption='[[1ek0]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1ek0]] 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=1EK0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EK0 FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.48&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MHO:S-OXYMETHIONINE'>MHO</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr>
-{{STRUCTURE_1ek0|  PDB=1ek0  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ek0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ek0 OCA], [https://pdbe.org/1ek0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ek0 RCSB], [https://www.ebi.ac.uk/pdbsum/1ek0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ek0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/VPS21_YEAST VPS21_YEAST] Required for protein transport to the vacuole. Involved in two vesicle trafficking steps to the prevacuolar compartment (PVC), regulating the docking of endosomes and Golgi vesicles to the PVC by interacting with PEP7/VAC1 on the PVC membrane and promoting SNARE complex formation.<ref>PMID:10679018</ref> <ref>PMID:8137814</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/ek/1ek0_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=1ek0 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Ypt/Rab proteins are membrane-associated small GTP-binding proteins which play a central role in the coordination, activation and regulation of vesicle-mediated transport in eukaryotic cells. We present the 1.5 A high-resolution crystal structure of Ypt51 in its active, GppNHp-bound conformation. Ypt51 is an important regulator involved in the endocytic membrane traffic of Saccharomyces cerevisiae. The structure reveals small but significant structural differences compared with H-Ras p21. The effector loop and the catalytic loop are well defined and stabilized by extensive hydrophobic interactions. The switch I and switch II regions form a well-defined epitope for hypothetical effector protein binding. Sequence comparisons between the different isoforms Ypt51, Ypt52 and Ypt53 provide the first insights into determinants for specific effector binding and for fine-tuning of the intrinsic GTP-hydrolysis rate.
-===GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION===
+High-resolution crystal structure of S. cerevisiae Ypt51(DeltaC15)-GppNHp, a small GTP-binding protein involved in regulation of endocytosis.,Esters H, Alexandrov K, Constantinescu AT, Goody RS, Scheidig AJ J Mol Biol. 2000 Apr 21;298(1):111-21. PMID:10756108<ref>PMID:10756108</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1ek0" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_10756108}}, adds the Publication Abstract to the page
+*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 10756108 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_10756108}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-EK0 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EK0 OCA].
-==Reference==
-<ref group="xtra">PMID:10756108</ref><references group="xtra"/>
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Esters, H.]]
+[[Category: Esters H]]
-[[Category: Scheidig, A J.]]
+[[Category: Scheidig AJ]]
-[[Category: Endocytosis]]
-[[Category: G protein]]
-[[Category: Gtp hydrolysis]]
-[[Category: Hydrolase]]
-[[Category: Vesicular traffic]]
-[[Category: Ypt/rab protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 00:07:59 2009''