5h6b

Crystal structure of a thermostable lipase from Marine Streptomyces

spinqualitylabelsall models 5h6b, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5h6b is a 1 chain structure with sequence from Streptomyces sp. W007. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.3Å Ligands: ACT, IMD, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H0B8D4_9ACTN Publication Abstract from PubMed MAS1 from marine Streptomyces sp. strain W007 belongs to the bacterial lipase I.7 subfamily, and is characterized as a thermostable and non-regiospecific lipase. To shed light on the catalytic mechanism of MAS1, we determined its crystal structure with closed conformation in two crystal forms at 2.3-A resolution. MAS1 adopts the canonical alpha/beta hydrolase core fold with its catalytic triad being formed by S109, D200 and H232. Structural analysis and biochemical assays revealed that disulfide bonds and salt bridges play a vital role in the thermostability of MAS1. Additionally, we discovered that the substitution of H108 with a tryptophan converts MAS1 from a non-regiospecific to an sn-1, 3 specific lipase, suggesting the functional importance of the second position from the conserved pentapeptide motif in defining the regiospecificity of MAS1. Our present study provides insights into the molecular basis for the thermostability and regiospecificity of MAS1, and may aid in the rational design of thermostable or regiospecific lipases for potential industrial applications. This article is protected by copyright. All rights reserved. Crystal structure of a lipase from Streptomyces sp. strain W007:implications for thermostability and regiospecificity.,Zhao Z, Hou S, Lan D, Wang X, Liu J, Khan FI, Wang Y FEBS J. 2017 Aug 31. doi: 10.1111/febs.14211. PMID:28857479 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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