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| | ==SOLUTION STRUCTURE OF APO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY== | | ==SOLUTION STRUCTURE OF APO-BIOTINYL DOMAIN FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOPY== |
| - | <StructureSection load='3bdo' size='340' side='right'caption='[[3bdo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='3bdo' size='340' side='right'caption='[[3bdo]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3bdo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecobd Ecobd]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BDO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3BDO FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3bdo]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_BL21(DE3) Escherichia coli BL21(DE3)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BDO FirstGlance]. <br> |
| - | </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_carboxylase Acetyl-CoA carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.2 6.4.1.2] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bdo OCA], [http://pdbe.org/3bdo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bdo RCSB], [http://www.ebi.ac.uk/pdbsum/3bdo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bdo ProSAT]</span></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=3bdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bdo OCA], [https://pdbe.org/3bdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bdo RCSB], [https://www.ebi.ac.uk/pdbsum/3bdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bdo ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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. | + | [https://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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Acetyl-CoA carboxylase]] | |
| - | [[Category: Ecobd]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Broadhurst, R W]] | + | [[Category: Broadhurst RW]] |
| - | [[Category: Chapman-Smith, A]] | + | [[Category: Chapman-Smith A]] |
| - | [[Category: Cronan, J E]] | + | [[Category: Cronan JE]] |
| - | [[Category: Howard, M J]] | + | [[Category: Howard MJ]] |
| - | [[Category: Morris, T]] | + | [[Category: Morris T]] |
| - | [[Category: Perham, R N]] | + | [[Category: Perham RN]] |
| - | [[Category: Roberts, E L]] | + | [[Category: Roberts EL]] |
| - | [[Category: Shu, N]] | + | [[Category: Shu N]] |
| - | [[Category: Wallace, J C]] | + | [[Category: Wallace JC]] |
| - | [[Category: Acetyl coa carboxylase]]
| + | |
| - | [[Category: Biotin]]
| + | |
| - | [[Category: Biotinyl domain]]
| + | |
| - | [[Category: Nmr spectroscopy]]
| + | |
| - | [[Category: Protein structure]]
| + | |
| - | [[Category: Swinging arm]]
| + | |
| Structural highlights
Function
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
A subgene encoding the 87 C-terminal amino acids of the biotinyl carboxy carrier protein (BCCP) from the acetyl CoA carboxylase of Escherichia coli was overexpressed and the apoprotein biotinylated in vitro. The structures of both the apo and holo forms of the biotinyl domain were determined by means of multidimensional NMR spectroscopy. That of the holo domain was well-defined, except for the 10 N-terminal residues, which form part of the flexible linker between the biotinyl and subunit-binding domains of BCCP. In agreement with X-ray crystallographic studies [Athappilly, F. K., and Hendrickson, W. A. (1995) Structure 3, 1407-1419], the structure comprises a flattened beta-barrel composed of two four-stranded beta-sheets with a 2-fold axis of quasi-symmetry and the biotinyl-lysine residue displayed in an exposed beta-turn on the side of the protein opposite from the N- and C-terminal residues. The biotin group is immobilized on the protein surface, with the ureido ring held down by interactions with a protruding polypeptide "thumb" formed by residues 94-101. However, at the site of carboxylation, no evidence could be found in solution for the predicted hydrogen bond between the main chain O of Thr94 and the ureido HN1'. The structure of the apo domain is essentially identical, although the packing of side chains is more favorable in the holo domain, and this may be reflected in differences in the dynamics of the two forms. The thumb region appears to be lacking in almost all other biotinyl domain sequences, and it may be that the immobilization of the biotinyl-lysine residue in the biotinyl domain of BCCP is an unusual requirement, needed for the catalytic reaction of acetyl CoA carboxylase.
Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy.,Roberts EL, Shu N, Howard MJ, Broadhurst RW, Chapman-Smith A, Wallace JC, Morris T, Cronan JE Jr, Perham RN Biochemistry. 1999 Apr 20;38(16):5045-53. PMID:10213607[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Roberts EL, Shu N, Howard MJ, Broadhurst RW, Chapman-Smith A, Wallace JC, Morris T, Cronan JE Jr, Perham RN. Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy. Biochemistry. 1999 Apr 20;38(16):5045-53. PMID:10213607 doi:10.1021/bi982466o
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