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4hr7
From Proteopedia
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| - | + | ==Crystal Structure of Biotin Carboxyl Carrier Protein-Biotin Carboxylase Complex from E.coli== | |
| - | + | <StructureSection load='4hr7' size='340' side='right' caption='[[4hr7]], [[Resolution|resolution]] 2.50Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4hr7]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli_k-12 Escherichia coli k-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HR7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HR7 FirstGlance]. <br> | |
| - | ==Function== | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1dv1|1dv1]], [[1bdo|1bdo]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">accC, fabG, b3256, JW3224 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12]), accB, fabE, b3255, JW3223 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 Escherichia coli K-12])</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=4hr7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hr7 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hr7 RCSB], [http://www.ebi.ac.uk/pdbsum/4hr7 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/ACCC_ECOLI ACCC_ECOLI]] 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. [[http://www.uniprot.org/uniprot/BCCP_ECOLI BCCP_ECOLI]] 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. | [[http://www.uniprot.org/uniprot/ACCC_ECOLI ACCC_ECOLI]] 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. [[http://www.uniprot.org/uniprot/BCCP_ECOLI BCCP_ECOLI]] 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;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Acetyl-coenzyme A (acetyl-CoA) carboxylase is a biotin-dependent, multifunctional enzyme that catalyzes the regulated step in fatty acid synthesis. The Escherichia coli enzyme is composed of a homodimeric biotin carboxylase (BC), biotinylated biotin carboxyl carrier protein (BCCP), and an alpha2beta2 heterotetrameric carboxyltransferase. This enzyme complex catalyzes two half-reactions to form malonyl-coenzyme A. BC and BCCP participate in the first half-reaction, whereas carboxyltransferase and BCCP are involved in the second. Three-dimensional structures have been reported for the individual subunits; however, the structural basis for how BCCP reacts with the carboxylase or transferase is unknown. Therefore, we report here the crystal structure of E. coli BCCP complexed with BC to a resolution of 2.49 A. The protein-protein complex shows a unique quaternary structure and two distinct interfaces for each BCCP monomer. These BCCP binding sites are unique compared to phylogenetically related biotin-dependent carboxylases and therefore provide novel targets for developing antibiotics against bacterial acetyl-CoA carboxylase. | ||
| + | |||
| + | The Three-Dimensional Structure of the Biotin Carboxylase-Biotin Carboxyl Carrier Protein Complex of E. coli Acetyl-CoA Carboxylase.,Broussard TC, Kobe MJ, Pakhomova S, Neau DB, Price AE, Champion TS, Waldrop GL Structure. 2013 Mar 12. pii: S0969-2126(13)00041-5. doi:, 10.1016/j.str.2013.02.001. PMID:23499019<ref>PMID:23499019</ref> | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | + | *[[Biotin carboxylase|Biotin carboxylase]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Escherichia coli k-12]] | [[Category: Escherichia coli k-12]] | ||
| - | [[Category: Broussard, T C | + | [[Category: Broussard, T C]] |
| - | [[Category: Champion, T S | + | [[Category: Champion, T S]] |
| - | [[Category: Kobe, M J | + | [[Category: Kobe, M J]] |
| - | [[Category: Neau, D B | + | [[Category: Neau, D B]] |
| - | [[Category: Pakhomova, S | + | [[Category: Pakhomova, S]] |
| - | [[Category: Price, A E | + | [[Category: Price, A E]] |
| - | [[Category: Waldrop, G L | + | [[Category: Waldrop, G L]] |
[[Category: Acetyl-coa carboxylase]] | [[Category: Acetyl-coa carboxylase]] | ||
[[Category: Antibiotic target]] | [[Category: Antibiotic target]] | ||
Revision as of 09:38, 25 December 2014
Crystal Structure of Biotin Carboxyl Carrier Protein-Biotin Carboxylase Complex from E.coli
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Categories: Escherichia coli k-12 | Broussard, T C | Champion, T S | Kobe, M J | Neau, D B | Pakhomova, S | Price, A E | Waldrop, G L | Acetyl-coa carboxylase | Antibiotic target | Atp grasp | Biotin carboxyl carrier protein | Biotin carboxylase | Biotin-dependent carboxylase | Fatty acid synthesis | Ligase-biotin binding protein complex | Protein complex | Protein interface | Protein-protein interaction
