2af8
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ACTINORHODIN POLYKETIDE SYNTHASE ACYL CARRIER PROTEIN FROM STREPTOMYCES COELICOLOR A3(2), NMR, MINIMIZED AVERAGE STRUCTURE
OverviewOverview
The solution structure of the actinorhodin acyl carrier protein (act, apo-ACP) from the polyketide synthase (PKS) of Streptomyces coelicolor, A3(2) has been determined using 1H NMR spectroscopy, representing the, first polyketide synthase component for which detailed structural, information has been obtained. Twenty-four structures were generated by, simulated annealing, employing 699 distance restraints and 94 dihedral, angle restraints. The structure is composed, principally, of three major, helices (1, 2, and 4), a shorter helix (3) and a large loop region, separating helices 1 and 2. The structure is well-defined, except for a, portion of the loop region (residues 18-29), the N-terminus (1-4), and a, short stretch (57-61) in the loop connecting helices 2 and 3. The RMS, distribution ... [(full description)]
About this StructureAbout this Structure
2AF8 is a [Single protein] structure of sequence from [Streptomyces coelicolor]. Structure known Active Site: S42. Full crystallographic information is available from [OCA].
ReferenceReference
Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3(2)., Crump MP, Crosby J, Dempsey CE, Parkinson JA, Murray M, Hopwood DA, Simpson TJ, Biochemistry. 1997 May 20;36(20):6000-8. PMID:9166770
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