6arf: Difference between revisions
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<StructureSection load='6arf' size='340' side='right'caption='[[6arf]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='6arf' size='340' side='right'caption='[[6arf]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6arf]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ARF OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6arf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus_Af293 Aspergillus fumigatus Af293]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ARF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ARF FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.702Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene></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=6arf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6arf OCA], [https://pdbe.org/6arf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6arf RCSB], [https://www.ebi.ac.uk/pdbsum/6arf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6arf ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ER10B_ASPFU ER10B_ASPFU] 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) (Ref.6). Erg10B catalyzes the formation of acetoacetyl-CoA from acetyl-CoA (Ref.6). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase erg10B that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13A and erg13B then condense 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. Mevalonate is also a precursor for the extracellular siderophore triacetylfusarinine C (TAFC) (PubMed:16110826, PubMed:22106303) (Probable).<ref>PMID:17352532</ref> <ref>PMID:16110826</ref> <ref>PMID:22106303</ref> | |||
==See Also== | |||
*[[Thiolase 3D structures|Thiolase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aspergillus fumigatus Af293]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Bond | [[Category: Bond CS]] | ||
[[Category: Bruning | [[Category: Bruning JB]] | ||
[[Category: Marshall | [[Category: Marshall AC]] | ||
Latest revision as of 17:18, 13 March 2024
Aspergillus fumigatus Cytosolic Thiolase: Apo enzyme in complex with potassium ionsAspergillus fumigatus Cytosolic Thiolase: Apo enzyme in complex with potassium ions
Structural highlights
FunctionER10B_ASPFU 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) (Ref.6). Erg10B catalyzes the formation of acetoacetyl-CoA from acetyl-CoA (Ref.6). The first module starts with the action of the cytosolic acetyl-CoA acetyltransferase erg10B that catalyzes the formation of acetoacetyl-CoA. The hydroxymethylglutaryl-CoA synthases erg13A and erg13B then condense 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. Mevalonate is also a precursor for the extracellular siderophore triacetylfusarinine C (TAFC) (PubMed:16110826, PubMed:22106303) (Probable).[1] [2] [3] See AlsoReferences
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