1h8m: Difference between revisions
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==Solution structure of ykt6== | |||
<StructureSection load='1h8m' size='340' side='right'caption='[[1h8m]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1h8m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H8M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H8M FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1h8m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h8m OCA], [https://pdbe.org/1h8m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h8m RCSB], [https://www.ebi.ac.uk/pdbsum/1h8m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h8m ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/YKT6_YEAST YKT6_YEAST] | |||
== 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/h8/1h8m_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1h8m ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ykt6p is a nonsyntaxin SNARE implicated in multiple intracellular membrane trafficking steps. Here we present the structure of the NH2-terminal domain of Ykt6p (Ykt6pN, residues 1 to 140). The structure of Ykt6pN differed entirely from that of syntaxin and resembled the overall fold of the actin regulatory protein, profilin. Like some syntaxins, Ykt6p adopted a folded back conformation in which Ykt6pN bound to its COOH-terminal core domain. The NH2-terminal domain plays an important biological role in the function of Ykt6p, which in vitro studies revealed to include influencing the kinetics and proper assembly of SNARE complexes. | |||
An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p.,Tochio H, Tsui MM, Banfield DK, Zhang M Science. 2001 Jul 27;293(5530):698-702. PMID:11474112<ref>PMID:11474112</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1h8m" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Banfield | [[Category: Banfield DK]] | ||
[[Category: Tochio | [[Category: Tochio H]] | ||
[[Category: Tsui | [[Category: Tsui MMK]] | ||
[[Category: Zhang | [[Category: Zhang M]] | ||
Latest revision as of 08:31, 15 May 2024
Solution structure of ykt6Solution structure of ykt6
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedYkt6p is a nonsyntaxin SNARE implicated in multiple intracellular membrane trafficking steps. Here we present the structure of the NH2-terminal domain of Ykt6p (Ykt6pN, residues 1 to 140). The structure of Ykt6pN differed entirely from that of syntaxin and resembled the overall fold of the actin regulatory protein, profilin. Like some syntaxins, Ykt6p adopted a folded back conformation in which Ykt6pN bound to its COOH-terminal core domain. The NH2-terminal domain plays an important biological role in the function of Ykt6p, which in vitro studies revealed to include influencing the kinetics and proper assembly of SNARE complexes. An autoinhibitory mechanism for nonsyntaxin SNARE proteins revealed by the structure of Ykt6p.,Tochio H, Tsui MM, Banfield DK, Zhang M Science. 2001 Jul 27;293(5530):698-702. PMID:11474112[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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