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2KOR

NMR solution structures of 2-octenoyl-ACP from Streptomyces coelicolor Fatty Acid Synthase

Summary for 2KOR
Entry DOI10.2210/pdb2kor/pdb
Related2kOO 2kOP 2kOQ 2kOS
NMR InformationBMRB: 16527
DescriptorAcyl carrier protein, S-[2-[3-[[(2S)-2-hydroxy-3,3-dimethyl-4-phosphonooxy-butanoyl]amino]propanoylamino]ethyl] (E)-oct-2-enethioate (2 entities in total)
Functional Keywordsacyl carrier protein, intermediate binding, fatty acid synthase, fatty acid biosynthesis, lipid synthesis, phosphopantetheine, transport protein
Biological sourceStreptomyces coelicolor
Cellular locationCytoplasm (By similarity): P72393
Total number of polymer chains1
Total formula weight9276.30
Authors
Ploskon, E.,Arthur, C.J.,Crump, M.P. (deposition date: 2009-09-29, release date: 2010-08-18, Last modification date: 2024-11-13)
Primary citationPloskon, E.,Arthur, C.J.,Kanari, A.L.,Wattana-amorn, P.,Williams, C.,Crosby, J.,Simpson, T.J.,Willis, C.L.,Crump, M.P.
Recognition of intermediate functionality by acyl carrier protein over a complete cycle of fatty acid biosynthesis
Chem.Biol., 17:776-785, 2010
Cited by
PubMed Abstract: It remains unclear whether in a bacterial fatty acid synthase (FAS) acyl chain transfer is a programmed or diffusion controlled and random action. Acyl carrier protein (ACP), which delivers all intermediates and interacts with all synthase enzymes, is the key player in this process. High-resolution structures of intermediates covalently bound to an ACP representing each step in fatty acid biosynthesis have been solved by solution NMR. These include hexanoyl-, 3-oxooctanyl-, 3R-hydroxyoctanoyl-, 2-octenoyl-, and octanoyl-ACP from Streptomyces coelicolor FAS. The high-resolution structures reveal that the ACP adopts a unique conformation for each intermediate driven by changes in the internal fatty acid binding pocket. The binding of each intermediate shows conserved structural features that may ensure effective molecular recognition over subsequent rounds of fatty acid biosynthesis.
PubMed: 20659690
DOI: 10.1016/j.chembiol.2010.05.024
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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