1A6X
STRUCTURE OF THE APO-BIOTIN CARBOXYL CARRIER PROTEIN (APO-BCCP87) OF ESCHERICHIA COLI ACETYL-COA CARBOXYLASE, NMR, 49 STRUCTURES
Summary for 1A6X
| Entry DOI | 10.2210/pdb1a6x/pdb |
| Descriptor | APO-BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE (1 entity in total) |
| Functional Keywords | acetyl-coa carboxylase, biotin carboxyl carrier protein, backbone dynamics, carrier protein |
| Biological source | Escherichia coli BL21(DE3) |
| Total number of polymer chains | 1 |
| Total formula weight | 9341.75 |
| Authors | Yao, X.,Wei, D.,Soden Junior, C.,Summers, M.F.,Beckett, D. (deposition date: 1998-03-04, release date: 1998-10-14, Last modification date: 2024-05-22) |
| Primary citation | Yao, X.,Wei, D.,Soden Jr., C.,Summers, M.F.,Beckett, D. Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase. Biochemistry, 36:15089-15100, 1997 Cited by PubMed Abstract: The biotin carboxyl carrier protein (BCCP) is a subunit of acetyl-CoA carboxylase, a biotin-dependent enzyme that catalyzes the first committed step of fatty acid biosynthesis. In its functional cycle the biotin carboxyl carrier protein engages in heterologous protein-protein interactions with three distinct partners, depending on its state of posttranslational modification. Apo-BCCP interacts specifically with the biotin holoenzyme synthetase, BirA, which results in the posttranslational attachment of biotin to an essential lysine residue on BCCP. Holo-BCCP then interacts with the biotin carboxylase subunit, which leads to the addition of the carboxylate group of bicarbonate to biotin. Finally, the carboxybiotinylated form of BCCP interacts with transcarboxylase in the conversion of acetyl-CoA to malonyl-CoA. The determinants of protein-protein interaction specificity in this system are unknown. One hypothesis is that posttranslational modification of BCCP may result in conformational changes that regulate specific protein-protein interactions. To test this hypothesis, we have determined the NMR solution structure of the unbiotinylated form of an 87 residue C-terminal domain fragment of BCCP (apoBCCP87) from Escherichia coli acetyl-CoA carboxylase and compared this structure with the high-resolution structure of the biotinylated form that was recently solved by X-ray crystallographic techniques. Although the overall folding of the two proteins is highly similar, small structural differences are apparent for residues of the biotin-binding loop that may be important for mediating specific protein-protein interactions. PubMed: 9398236DOI: 10.1021/bi971485f PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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