Structural highlights
Publication Abstract from PubMedMAS1 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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