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2ahu

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==Crystal structure of Acyl-CoA transferase (YdiF) apoenzyme from Escherichia coli O157:H7.==
==Crystal structure of Acyl-CoA transferase (YdiF) apoenzyme from Escherichia coli O157:H7.==
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<StructureSection load='2ahu' size='340' side='right' caption='[[2ahu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='2ahu' size='340' side='right'caption='[[2ahu]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2ahu]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AHU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2ahu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Eco57 Eco57]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AHU FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ahv|2ahv]], [[2ahw|2ahw]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ahv|2ahv]], [[2ahw|2ahw]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YdiF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YdiF ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83334 ECO57])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ahu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahu OCA], [http://pdbe.org/2ahu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ahu RCSB], [http://www.ebi.ac.uk/pdbsum/2ahu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ahu ProSAT]</span></td></tr>
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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=2ahu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahu OCA], [https://pdbe.org/2ahu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ahu RCSB], [https://www.ebi.ac.uk/pdbsum/2ahu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ahu ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/YDIF_ECO57 YDIF_ECO57]] CoA transferase having broad substrate specificity for short-chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons. Exhibits high activity with acetoacetyl-CoA, propionyl-CoA, crotonoyl-CoA or butyryl-CoA as donors, with acetate as an acceptor. When acetyl-CoA is used as the donor, propionate, acetoacetate, butyrate, isobutyrate, and 4-hydroxybutyrate can be utilized as acceptors but not isovalerate. May play a role in short-chain fatty acid metabolism in E.coli.<ref>PMID:16253988</ref>
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[[https://www.uniprot.org/uniprot/YDIF_ECO57 YDIF_ECO57]] CoA transferase having broad substrate specificity for short-chain acyl-CoA thioesters with the activity decreasing when the length of the carboxylic acid chain exceeds four carbons. Exhibits high activity with acetoacetyl-CoA, propionyl-CoA, crotonoyl-CoA or butyryl-CoA as donors, with acetate as an acceptor. When acetyl-CoA is used as the donor, propionate, acetoacetate, butyrate, isobutyrate, and 4-hydroxybutyrate can be utilized as acceptors but not isovalerate. May play a role in short-chain fatty acid metabolism in E.coli.<ref>PMID:16253988</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Eco57]]
[[Category: Eco57]]
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[[Category: Large Structures]]
[[Category: Ajamian, E]]
[[Category: Ajamian, E]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]

Revision as of 08:31, 27 January 2021

Crystal structure of Acyl-CoA transferase (YdiF) apoenzyme from Escherichia coli O157:H7.

PDB ID 2ahu

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