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==Human START domain of Acyl-coenzyme A thioesterase 11 (ACOT11)==
==Human START domain of Acyl-coenzyme A thioesterase 11 (ACOT11)==
<StructureSection load='3fo5' size='340' side='right' caption='[[3fo5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='3fo5' size='340' side='right'caption='[[3fo5]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3fo5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FO5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FO5 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3fo5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FO5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FO5 FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TCE:3,3,3-PHOSPHANETRIYLTRIPROPANOIC+ACID'>TCE</scene><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]] 2&#8491;</td></tr>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACOT11, hCG_33028, RP11-240D10.1-002 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1PE:PENTAETHYLENE+GLYCOL'>1PE</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=TCE:3,3,3-PHOSPHANETRIYLTRIPROPANOIC+ACID'>TCE</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=3fo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fo5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fo5 RCSB], [http://www.ebi.ac.uk/pdbsum/3fo5 PDBsum]</span></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=3fo5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fo5 OCA], [https://pdbe.org/3fo5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fo5 RCSB], [https://www.ebi.ac.uk/pdbsum/3fo5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fo5 ProSAT]</span></td></tr>
<table>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACO11_HUMAN ACO11_HUMAN] Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/3fo5_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fo/3fo5_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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=3fo5 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Steroidogenic acute regulatory (StAR) protein related lipid transfer (START) domains are small globular modules that form a cavity where lipids and lipid hormones bind. These domains can transport ligands to facilitate lipid exchange between biological membranes, and they have been postulated to modulate the activity of other domains of the protein in response to ligand binding. More than a dozen human genes encode START domains, and several of them are implicated in a disease. PRINCIPAL FINDINGS: We report crystal structures of the human STARD1, STARD5, STARD13 and STARD14 lipid transfer domains. These represent four of the six functional classes of START domains. SIGNIFICANCE: Sequence alignments based on these and previously reported crystal structures define the structural determinants of human START domains, both those related to structural framework and those involved in ligand specificity. ENHANCED VERSION: This article can also be viewed as an enhanced version in which the text of the article is integrated with interactive 3D representations and animated transitions. Please note that a web plugin is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available in Text S1.
Comparative structural analysis of lipid binding START domains.,Thorsell AG, Lee WH, Persson C, Siponen MI, Nilsson M, Busam RD, Kotenyova T, Schuler H, Lehtio L PLoS One. 2011;6(6):e19521. Epub 2011 Jun 30. PMID:21738568<ref>PMID:21738568</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Thioesterase|Thioesterase]]
*[[Thioesterase 3D structures|Thioesterase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Arrowsmith, C H.]]
[[Category: Large Structures]]
[[Category: Berglund, H.]]
[[Category: Arrowsmith CH]]
[[Category: Bountra, C.]]
[[Category: Berglund H]]
[[Category: Collins, R.]]
[[Category: Bountra C]]
[[Category: Dahlgren, L G.]]
[[Category: Collins R]]
[[Category: Edwards, A M.]]
[[Category: Dahlgren LG]]
[[Category: Flodin, S.]]
[[Category: Edwards AM]]
[[Category: Flores, A.]]
[[Category: Flodin S]]
[[Category: Graslund, S.]]
[[Category: Flores A]]
[[Category: Hammarstrom, M.]]
[[Category: Graslund S]]
[[Category: Johansson, A.]]
[[Category: Hammarstrom M]]
[[Category: Johansson, I.]]
[[Category: Johansson A]]
[[Category: Karlberg, T.]]
[[Category: Johansson I]]
[[Category: Kotenyova, T.]]
[[Category: Karlberg T]]
[[Category: Lehtio, L.]]
[[Category: Kotenyova T]]
[[Category: Moche, M.]]
[[Category: Lehtio L]]
[[Category: Nilsson, M E.]]
[[Category: Moche M]]
[[Category: Nordlund, P.]]
[[Category: Nilsson ME]]
[[Category: Nyman, T.]]
[[Category: Nordlund P]]
[[Category: Persson, C.]]
[[Category: Nyman T]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Persson C]]
[[Category: Sagemark, J.]]
[[Category: Sagemark J]]
[[Category: Shueler, H.]]
[[Category: Shueler H]]
[[Category: Siponen, M I.]]
[[Category: Siponen MI]]
[[Category: Thorsell, A G.]]
[[Category: Thorsell AG]]
[[Category: Tresaugues, L.]]
[[Category: Tresaugues L]]
[[Category: Van-Den-Berg, S.]]
[[Category: Van-Den-Berg S]]
[[Category: Weigelt, J.]]
[[Category: Weigelt J]]
[[Category: Welin, M.]]
[[Category: Welin M]]
[[Category: Wikstrom, M.]]
[[Category: Wikstrom M]]
[[Category: Wisniewska, M.]]
[[Category: Wisniewska M]]
[[Category: Consortium]]
[[Category: Lipid transport]]
[[Category: Orthogonal bundle]]

Latest revision as of 11:25, 20 March 2024

Human START domain of Acyl-coenzyme A thioesterase 11 (ACOT11)Human START domain of Acyl-coenzyme A thioesterase 11 (ACOT11)

Structural highlights

3fo5 is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACO11_HUMAN Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

3fo5, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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