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Article

Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution.

Acta crystallographica. Section D, Biological crystallography - 1 Jul 2002

Kawasaki Kosei, Kondo Hidemasa, Suzuki Mamoru, Ohgiya Satoru, Tsuda Sakae

Abstract excerpt

Bacillus subtilis extracellular lipase (BsL) has an exceptionally low molecular weight (19.4 kDa) for a member of the lipase family. A crystallographic study was performed on BsL in order to design and produce mutant BsL that will be more suitable for industrial uses based on analysis of the three-dimensional structure. Recently, the crystal structure of BsL has been determined at 1.5 A resolution [van Pouderoyen...

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Identifiers

PMID: 12077437
DOI: 10.1107/s090744490200714x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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