2K94
Structural modification of acyl carrier protein by butyryl group
Summary for 2K94
Entry DOI | 10.2210/pdb2k94/pdb |
Related | 2K92 2K93 |
Descriptor | Acyl carrier protein (1 entity in total) |
Functional Keywords | butytyl form of acyl carrier protein, fatty acid synthesis protein, cytoplasm, fatty acid biosynthesis, lipid synthesis, phosphopantetheine, lipid transport |
Biological source | Escherichia coli |
Cellular location | Cytoplasm: P0A6A8 |
Total number of polymer chains | 1 |
Total formula weight | 8513.28 |
Authors | Wu, B.N. (deposition date: 2008-09-29, release date: 2009-01-20, Last modification date: 2024-05-22) |
Primary citation | Wu, B.N.,Zhang, Y.M.,Rock, C.O.,Zheng, J.J. Structural modification of acyl carrier protein by butyryl group. Protein Sci., 18:240-246, 2009 Cited by PubMed Abstract: Fatty acid synthesis in bacteria is catalyzed by a set of individual enzymes known as the type II fatty acid synthase. Acyl carrier protein (ACP) shuttles the acyl intermediates between individual pathway enzymes. In this study, we determined the solution structures of three different forms of ACP, apo-ACP, ACP, and butyryl-ACP under identical experimental conditions. The structural studies revealed that attachment of butyryl acyl intermediate to ACP alters the conformation of ACP. This finding supports the more general notion that the attachment of different acyl intermediates alters the ACP structure to facilitate their recognition and turnover by the appropriate target enzymes. PubMed: 19177367DOI: 10.1002/pro.11 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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