2kr5

Solution Structure of an Acyl Carrier Protein Domain from Fungal Type I Polyketide Synthase

spinqualitylabelsall models 2kr5, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2kr5 is a 1 chain structure with sequence from Aspergillus parasiticus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PNS Gene: pksL1 (Aspergillus parasiticus) Resources: FirstGlance, OCA, RCSB, PDBsum Function [PKSL1_ASPPA] Combines a hexanoyl starter unit and 7 malonyl-CoA extender units to synthesize the precursor norsolorinic acid anthrone (noranthrone) in the aflatoxin biosynthesis pathway. The hexanoyl starter unit is provided to the acyl-carrier protein (ACP) domain by a dedicated fungal fatty acid synthase. 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 Acyl (peptidyl) carrier protein (ACP or PCP) is a crucial component involved in the transfer of thiol ester-bound intermediates during the biosynthesis of primary and secondary metabolites such as fatty acids, polyketides, and nonribosomal peptides. Although many carrier protein three-dimensional structures have been determined, to date there is no model available for a fungal type I polyketide synthase ACP. Here we report the solution structure of the norsolorinic acid synthase (NSAS) holo ACP domain that has been excised from the full-length multifunctional enzyme. NSAS ACP shows similarities in three-dimensional structure with other type I and type II ACPs, consisting of a four-helix bundle with helices I, II, and IV arranged in parallel. The N-terminus of helix III, however, is unusually hydrophobic, and Phe1768 and Leu1770 pack well with the core of the protein. The result is that unlike other carrier proteins, helix III lies almost perpendicular to the three major helices. Helix III is well-defined by numerous NMR-derived distance restraints and may be less flexible than counterparts in type II FAS and PKS ACPs. When the holo ACP is derivatized with a hexanoyl group, only minor changes are observed between the HSQC spectra of the two ACP species and no NOEs are observed for this hydrophobic acyl group. Along with the mammalian type I FAS, this further strengthens the view that type I ACPs do not show any significant affinity for hydrophobic (nonpolar) chain assembly intermediates attached via the 4'-phosphopantetheine prosthetic group. Solution structure of an acyl carrier protein domain from a fungal type I polyketide synthase.,Wattana-amorn P, Williams C, Ploskon E, Cox RJ, Simpson TJ, Crosby J, Crump MP Biochemistry. 2010 Mar 16;49(10):2186-93. PMID:20136099 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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