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4rcn

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==Structure and function of a single-chain, multi-domain long-chain acyl-coa carboxylase==
==Structure and function of a single-chain, multi-domain long-chain acyl-coa carboxylase==
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<StructureSection load='4rcn' size='340' side='right' caption='[[4rcn]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
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<StructureSection load='4rcn' size='340' side='right'caption='[[4rcn]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4rcn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RCN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RCN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4rcn]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_avium_subsp._paratuberculosis_K-10 Mycobacterium avium subsp. paratuberculosis K-10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RCN FirstGlance]. <br>
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</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=4rcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rcn OCA], [http://pdbe.org/4rcn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rcn RCSB], [http://www.ebi.ac.uk/pdbsum/4rcn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rcn ProSAT]</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]] 3.01&#8491;</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=4rcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rcn OCA], [https://pdbe.org/4rcn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rcn RCSB], [https://www.ebi.ac.uk/pdbsum/4rcn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rcn ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q73VY8_MYCPA Q73VY8_MYCPA]
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Biotin-dependent carboxylases are widely distributed in nature and have important functions in the metabolism of fatty acids, amino acids, carbohydrates, cholesterol and other compounds. Defective mutations in several of these enzymes have been linked to serious metabolic diseases in humans, and acetyl-CoA carboxylase is a target for drug discovery in the treatment of diabetes, cancer and other diseases. Here we report the identification and biochemical, structural and functional characterizations of a novel single-chain (120 kDa), multi-domain biotin-dependent carboxylase in bacteria. It has preference for long-chain acyl-CoA substrates, although it is also active towards short-chain and medium-chain acyl-CoAs, and we have named it long-chain acyl-CoA carboxylase. The holoenzyme is a homo-hexamer with molecular mass of 720 kDa. The 3.0 A crystal structure of the long-chain acyl-CoA carboxylase holoenzyme from Mycobacterium avium subspecies paratuberculosis revealed an architecture that is strikingly different from those of related biotin-dependent carboxylases. In addition, the domains of each monomer have no direct contact with each other. They are instead extensively swapped in the holoenzyme, such that one cycle of catalysis involves the participation of four monomers. Functional studies in Pseudomonas aeruginosa suggest that the enzyme is involved in the utilization of selected carbon and nitrogen sources.
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Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase.,Tran TH, Hsiao YS, Jo J, Chou CY, Dietrich LE, Walz T, Tong L Nature. 2015 Feb 5;518(7537):120-4. doi: 10.1038/nature13912. Epub 2014 Nov 10. PMID:25383525<ref>PMID:25383525</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4rcn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Tong, L]]
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[[Category: Large Structures]]
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[[Category: Tran, T H]]
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[[Category: Mycobacterium avium subsp. paratuberculosis K-10]]
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[[Category: Acyl-coa carboxylase]]
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[[Category: Tong L]]
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[[Category: Alpha/beta]]
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[[Category: Tran TH]]
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[[Category: Carboxylase]]
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[[Category: Coa binding]]
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[[Category: Holoenzyme]]
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[[Category: Ligase]]
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[[Category: Protein structure]]
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Structure and function of a single-chain, multi-domain long-chain acyl-coa carboxylase

PDB ID 4rcn

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