6are

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:43, 2 April 2025) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Aspergillus fumigatus Cytosolic Thiolase in complex with two tetrahedral reaction intermediates and ammonium ions==
==Aspergillus fumigatus Cytosolic Thiolase in complex with two tetrahedral reaction intermediates and ammonium ions==
-
<StructureSection load='6are' size='340' side='right' caption='[[6are]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+
<StructureSection load='6are' size='340' side='right'caption='[[6are]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[6are]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ARE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ARE FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[6are]] 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=6ARE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ARE FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.75&#8491;</td></tr>
-
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene></td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NH4:AMMONIUM+ION'>NH4</scene>, <scene name='pdbligand=SCY:S-ACETYL-CYSTEINE'>SCY</scene></td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6aqp|6aqp]]</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=6are FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6are OCA], [https://pdbe.org/6are PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6are RCSB], [https://www.ebi.ac.uk/pdbsum/6are PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6are ProSAT]</span></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>
+
-
<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=6are FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6are OCA], [http://pdbe.org/6are PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6are RCSB], [http://www.ebi.ac.uk/pdbsum/6are PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6are ProSAT]</span></td></tr>
+
</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) (Probable) (PubMed:16110826, PubMed:22106303).<ref>PMID:17352532</ref> <ref>PMID:16110826</ref> <ref>PMID:22106303</ref>
==See Also==
==See Also==
-
*[[Thiolase|Thiolase]]
+
*[[Thiolase 3D structures|Thiolase 3D structures]]
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Acetyl-CoA C-acetyltransferase]]
+
[[Category: Aspergillus fumigatus Af293]]
-
[[Category: Bond, C S]]
+
[[Category: Large Structures]]
-
[[Category: Bruning, J B]]
+
[[Category: Bond CS]]
-
[[Category: Marshall, A C]]
+
[[Category: Bruning JB]]
-
[[Category: Claisen condensation]]
+
[[Category: Marshall AC]]
-
[[Category: Monovalent cation binding]]
+
-
[[Category: Reaction intermediate]]
+
-
[[Category: Thiolase]]
+
-
[[Category: Transferase]]
+

Current revision

Aspergillus fumigatus Cytosolic Thiolase in complex with two tetrahedral reaction intermediates and ammonium ions

PDB ID 6are

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6are"
Personal tools