Journal
FEBS LETTERS
Volume 581, Issue 26, Pages 5060-5064Publisher
WILEY
DOI: 10.1016/j.febslet.2007.09.048
Keywords
family i.3 lipase; crystal structure; closed; conformation; lid; Ca2+; binding site; pseudomonas sp; MIS38
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The crystal structure of a family I.3 lipase from Pseudomonas sp. MIS38 in a closed conformation was determined at 1.5 angstrom resolution. This structure highly resembles that of Serratia marcescens LipA in an open conformation, except for the structures of two lids. Lid1 is anchored by a Ca2+ ion (Ca1) in an open conformation, but lacks this Ca1 site and greatly changes its structure and position in a closed conformation. Lid2 forms a helical hairpin in an open conformation, but does not form it and covers the active site in a closed conformation. Based on these results, we discuss on the lid-opening mechanism. (C) 2007 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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