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1ky3

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[[Image:1ky3.jpg|left|200px]]
 
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{{Structure
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==GDP-BOUND YPT7P AT 1.35 A RESOLUTION==
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|PDB= 1ky3 |SIZE=350|CAPTION= <scene name='initialview01'>1ky3</scene>, resolution 1.35&Aring;
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<StructureSection load='1ky3' size='340' side='right'caption='[[1ky3]], [[Resolution|resolution]] 1.35&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5&#39;-DIPHOSPHATE'>GDP</scene>
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<table><tr><td colspan='2'>[[1ky3]] 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=1KY3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KY3 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35&#8491;</td></tr>
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|GENE= ypt7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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<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=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ky3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ky3 OCA], [https://pdbe.org/1ky3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ky3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ky3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ky3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/YPT7_YEAST YPT7_YEAST] Needed for homotypic vacuole fusion, the last step in the vacuole inheritance process.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ky/1ky3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ky3 ConSurf].
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<div style="clear:both"></div>
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'''GDP-BOUND YPT7P AT 1.35 A RESOLUTION'''
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==See Also==
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*[[GTP-binding protein 3D structures|GTP-binding protein 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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The GTPase Ypt7p from S. cerevisiae is involved in late endosome-to-vacuole transport and homotypic vacuole fusion. We present crystal structures of the GDP- and GppNHp-bound conformation of Ypt7p solved at 1.35 and 1.6 A resolution, respectively. Despite the similarity of the overall structure to other Ypt/Rab proteins, Ypt7p displays small but significant differences. The Ypt7p-specific residues Tyr33 and Tyr37 cause a difference in the main chain trace of the RabSF2 region and form a characteristic surface epitope. Ypt7p*GppNHp does not display the helix alpha2, characteristic of the Ras-superfamily, but instead possess an extended loop L4/L5. Due to insertions in loops L3 and L7, the neighboring RabSF1 and RabSF4 regions are different in their conformations to those of other Ypt/Rab proteins.
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[[Category: Large Structures]]
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==About this Structure==
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1KY3 is a [[Single protein]] 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=1KY3 OCA].
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==Reference==
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Rab-subfamily-specific regions of Ypt7p are structurally different from other RabGTPases., Constantinescu AT, Rak A, Alexandrov K, Esters H, Goody RS, Scheidig AJ, Structure. 2002 Apr;10(4):569-79. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11937061 11937061]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Single protein]]
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[[Category: Constantinescu A-T]]
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[[Category: Constantinescu, A T.]]
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[[Category: Rak A]]
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[[Category: Rak, A.]]
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[[Category: Scheidig AJ]]
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[[Category: Scheidig, A J.]]
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[[Category: GDP]]
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[[Category: MG]]
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[[Category: endocytosis]]
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[[Category: g protein]]
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[[Category: gtp hydrolysis]]
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[[Category: hydrolase]]
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[[Category: vesicular traffic]]
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[[Category: ypt/rab protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 12:33:12 2008''
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Current revision

GDP-BOUND YPT7P AT 1.35 A RESOLUTION

PDB ID 1ky3

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