4mv8: Difference between revisions
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==Crystal Structure of Biotin Carboxylase from Haemophilus influenzae in Complex with AMPPCP and Phosphate== | ==Crystal Structure of Biotin Carboxylase from Haemophilus influenzae in Complex with AMPPCP and Phosphate== | ||
<StructureSection load='4mv8' size='340' side='right' caption='[[4mv8]], [[Resolution|resolution]] 2.06Å' scene=''> | <StructureSection load='4mv8' size='340' side='right'caption='[[4mv8]], [[Resolution|resolution]] 2.06Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4mv8]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4mv8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Haemophilus_influenzae_Rd_KW20 Haemophilus influenzae Rd KW20]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MV8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MV8 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]] 2.06Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACP:PHOSPHOMETHYLPHOSPHONIC+ACID+ADENYLATE+ESTER'>ACP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=4mv8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mv8 OCA], [https://pdbe.org/4mv8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mv8 RCSB], [https://www.ebi.ac.uk/pdbsum/4mv8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mv8 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ACCC_HAEIN ACCC_HAEIN] This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4mv8" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4mv8" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Acetyl-CoA carboxylase 3D structures|Acetyl-CoA carboxylase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Haemophilus influenzae Rd KW20]] | ||
[[Category: Bonnot | [[Category: Large Structures]] | ||
[[Category: Broussard | [[Category: Bonnot RJ]] | ||
[[Category: Champion | [[Category: Broussard TC]] | ||
[[Category: Neau | [[Category: Champion TS]] | ||
[[Category: Pakhomova | [[Category: Neau DB]] | ||
[[Category: Waldrop | [[Category: Pakhomova S]] | ||
[[Category: Waldrop GL]] | |||
Latest revision as of 19:43, 20 September 2023
Crystal Structure of Biotin Carboxylase from Haemophilus influenzae in Complex with AMPPCP and PhosphateCrystal Structure of Biotin Carboxylase from Haemophilus influenzae in Complex with AMPPCP and Phosphate
Structural highlights
FunctionACCC_HAEIN This protein is a component of the acetyl coenzyme A carboxylase complex; first, biotin carboxylase catalyzes the carboxylation of the carrier protein and then the transcarboxylase transfers the carboxyl group to form malonyl-CoA. Publication Abstract from PubMedAcetyl-CoA carboxylase catalyzes the first and regulated step in fatty acid synthesis. In most Gram-negative and Gram-positive bacteria, the enzyme is composed of three proteins: biotin carboxylase, a biotin carboxyl carrier protein (BCCP), and carboxyltransferase. The reaction mechanism involves two half-reactions with biotin carboxylase catalyzing the ATP-dependent carboxylation of biotin-BCCP in the first reaction. In the second reaction, carboxyltransferase catalyzes the transfer of the carboxyl group from biotin-BCCP to acetyl-CoA to form malonyl-CoA. In this report, high-resolution crystal structures of biotin carboxylase from Haemophilus influenzae were determined with bicarbonate, the ATP analogue AMPPCP; the carboxyphosphate intermediate analogues, phosphonoacetamide and phosphonoformate; the products ADP and phosphate; and the carboxybiotin analogue N1'-methoxycarbonyl biotin methyl ester. The structures have a common theme in that bicarbonate, phosphate, and the methyl ester of the carboxyl group of N1'-methoxycarbonyl biotin methyl ester all bound in the same pocket in the active site of biotin carboxylase and as such utilize the same set of amino acids for binding. This finding suggests a catalytic mechanism for biotin carboxylase in which the binding pocket that binds tetrahedral phosphate also accommodates and stabilizes a tetrahedral dianionic transition state resulting from direct transfer of CO2 from the carboxyphosphate intermediate to biotin. Structural Analysis of Substrate, Reaction Intermediate, and Product Binding in Haemophilus influenzae Biotin Carboxylase.,Broussard TC, Pakhomova S, Neau DB, Bonnot R, Waldrop GL Biochemistry. 2015 Jun 9. PMID:26020841[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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