2ewn
From Proteopedia
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| - | [[Image:2ewn.gif|left|200px]] | + | [[Image:2ewn.gif|left|200px]] |
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| - | '''Ecoli Biotin Repressor with co-repressor analog''' | + | {{Structure |
| + | |PDB= 2ewn |SIZE=350|CAPTION= <scene name='initialview01'>2ewn</scene>, resolution 2.80Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=BTX:((2R,3S,4R,5R)-5-(6-AMINO-9H-PURIN-9-YL)-3,4-DIHYDROXY-TETRAHYDROFURAN-2-YL)METHYL 5-((3AS,4S,6AR)-2-OXO-HEXAHYDRO-1H-THIENO[3,4-D]IMIDAZOL-4-YL)PENTYL HYDROGEN PHOSPHATE'>BTX</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Biotin--[acetyl-CoA-carboxylase]_ligase Biotin--[acetyl-CoA-carboxylase] ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.15 6.3.4.15] | ||
| + | |GENE= birA, bioR, dhbB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | }} | ||
| + | |||
| + | '''Ecoli Biotin Repressor with co-repressor analog''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2EWN is a [ | + | 2EWN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EWN OCA]. |
==Reference== | ==Reference== | ||
| - | Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution., Wood ZA, Weaver LH, Brown PH, Beckett D, Matthews BW, J Mol Biol. 2006 Mar 24;357(2):509-23. Epub 2006 Jan 6. PMID:[http:// | + | Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution., Wood ZA, Weaver LH, Brown PH, Beckett D, Matthews BW, J Mol Biol. 2006 Mar 24;357(2):509-23. Epub 2006 Jan 6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16438984 16438984] |
[[Category: Biotin--[acetyl-CoA-carboxylase] ligase]] | [[Category: Biotin--[acetyl-CoA-carboxylase] ligase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
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[[Category: helix-turn-helix]] | [[Category: helix-turn-helix]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:45:19 2008'' |
Revision as of 14:45, 20 March 2008
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| , resolution 2.80Å | |||||||
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| Ligands: | |||||||
| Gene: | birA, bioR, dhbB (Escherichia coli) | ||||||
| Activity: | [acetyl-CoA-carboxylase_ligase Biotin--[acetyl-CoA-carboxylase] ligase], with EC number 6.3.4.15 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Ecoli Biotin Repressor with co-repressor analog
Overview
BirA catalyzes the adenylation and subsequent covalent attachment of biotin to the biotin carboxyl carrier protein (BCCP). In the absence of apo-BCCP, biotin-5'-AMP acts as a co-repressor that induces BirA dimerization and binding to the bio operator to repress biotin biosynthesis. The crystal structures of apo-BirA, and BirA in complex with biotin have been reported. We here describe the 2.8A resolution crystal structure of BirA in complex with the co-repressor analog biotinol-5'-AMP. It was previously shown that the structure of apo-BirA is monomeric and that binding of biotin weakly induces a dimeric structure in which three disordered surface loops become organized to form the dimer interface. The structure of the co-repressor complex is also a dimer, clearly related to the BirA.biotin structure, but with several significant conformational changes. A hitherto disordered "adenylate binding loop" forms a well-defined structure covering the co-repressor. The co-repressor buttresses the dimer interface, resulting in improved packing and a 12 degrees change in the hinge-bending angle along the dimer interface relative to the BirA.biotin structure. This helps explain why the binding of the co-repressor is necessary to optimize the binding of BirA to the bioO operator. The structure reveals an unexpected use of the nucleotide-binding motif GXGXXG in binding adenylate and controlling the repressor function. Finally, based on structural analysis we propose that the class of adenylating enzymes represented by BirA, lipoate protein ligase and class II tRNA synthetases diverged early and were selected based on their ability to sequester co-factors or amino acid residues, and adenylation activity arose independently through functional convergence.
About this Structure
2EWN is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Co-repressor induced order and biotin repressor dimerization: a case for divergent followed by convergent evolution., Wood ZA, Weaver LH, Brown PH, Beckett D, Matthews BW, J Mol Biol. 2006 Mar 24;357(2):509-23. Epub 2006 Jan 6. PMID:16438984 [[Category: Biotin--[acetyl-CoA-carboxylase] ligase]]
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