2liw | pdb_00002liw

NMR structure of HMG-ACPI domain from CurA module from Lyngbya majuscula

spinqualitylabelsall models 2liw, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2liw is a 1 chain structure with sequence from Lyngbya majuscula. Full experimental information is available from OCA. Related: 2liu Activity: Glucokinase, with EC number 2.7.1.2 Publication Abstract from PubMed Polyketide synthases (PKS) and non-ribosomal peptide synthetases (NRPS) are large multidomain proteins present in microorganisms that produce bioactive compounds. Curacin A is such a bioactive compound with potent anti-proliferative activity. During its biosynthesis the growing substrate is bound covalently to an acyl carrier protein (ACP) that is able to access catalytic sites of neighboring domains for chain elongation and modification. While ACP domains usually occur as monomers, the curacin A cluster codes for a triplet ACP(ACP<sub>I</sub>-ACP<sub>II</sub>-ACP<sub>III</sub>) within the CurA PKS module. We have determined the structure of the isolated holo ACP<sub>I</sub> and show that the ACPs are independent of each other within this tridomain system. In addition, we have determined the structure of the 3-hydroxyl-3-methylglutaryl-loaded holo-ACP<sub>I</sub>, which is the substrate for the unique halogenase (Hal) domain embedded within the CurA module. We have identified the interaction surface of both proteins using mutagenesis and MALDI-based identification of product formation. Amino acids affecting product formation are located on helices II and III of ACP<sub>I</sub> and form a contiguous surface. Since the CurA Hal accepts substrate only when presented by one of the ACPs within the ACP<sub>I</sub>-ACP<sub>II</sub>-ACP<sub>III</sub> tridomain, our data provide insight into the specificity of the chlorination reaction. Characterization of molecular interactions between ACP and halogenase domains in the curacin A polyketide synthase.,Busche AE, Gottstein D, Hein C, Ripin N, Pader I, Tufar P, Eisman EB, Gu L, Walsh CT, Loehr F, Sherman DH, Guntert P, Dotsch V ACS Chem Biol. 2011 Nov 21. PMID:22103656 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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