5xz5

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Current revision (08:17, 22 November 2023) (edit) (undo)
 
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<StructureSection load='5xz5' size='340' side='right'caption='[[5xz5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='5xz5' size='340' side='right'caption='[[5xz5]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5xz5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XZ5 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5XZ5 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5xz5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XZ5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XZ5 FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acetyltransferase Acetyl-CoA C-acetyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.9 2.3.1.9] </span></td></tr>
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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]] 2.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5xz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xz5 OCA], [http://pdbe.org/5xz5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xz5 RCSB], [http://www.ebi.ac.uk/pdbsum/5xz5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xz5 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=5xz5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xz5 OCA], [https://pdbe.org/5xz5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xz5 RCSB], [https://www.ebi.ac.uk/pdbsum/5xz5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xz5 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/THIL_YEAST THIL_YEAST]] Catalyzes the formation of acetoacetyl-CoA in the biosynthesis of mevalonate, an intermediate required for the biosynthesis of sterols and nonsterol isoprenoids.
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[https://www.uniprot.org/uniprot/ERG10_YEAST ERG10_YEAST] Acetyl-CoA acetyltransferase; part of the first module of ergosterol biosynthesis pathway that includes the early steps of the pathway, conserved across all eukaryotes, and which results in the formation of mevalonate from acetyl-coenzyme A (acetyl-CoA) (PubMed:7989303, PubMed:5571829). ERG10 catalyzes the formation of acetoacetyl-CoA from acetyl-CoA (PubMed:7989303, PubMed:5571829). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase ERG10 that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthase ERG13 then condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA. The rate-limiting step of the early module is the reduction to mevalonate by the 3-hydroxy-3-methylglutaryl-coenzyme A (HMG-CoA) reductases HMG1 and HMG2 which are derived from a single ancestral HMGR gene by gene duplication (PubMed:32679672).<ref>PMID:5571829</ref> <ref>PMID:7989303</ref> <ref>PMID:32679672</ref>
==See Also==
==See Also==
*[[Thiolase 3D structures|Thiolase 3D structures]]
*[[Thiolase 3D structures|Thiolase 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Acetyl-CoA C-acetyltransferase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Zhou, P F]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Zhu, Z L]]
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[[Category: Zhou PF]]
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[[Category: Acetoacetyl-coa thiolase]]
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[[Category: Zhu ZL]]
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[[Category: Claisen condension]]
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[[Category: The mevalonate pathway]]
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[[Category: Transferase]]
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Current revision

Purification,crystallization and structural analysis of cytoplastic acetoacetyl-CoA thiolase from Saccharomyces cerevisiae

PDB ID 5xz5

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