1I6W

THE CRYSTAL STRUCTURE OF BACILLUS SUBTILIS LIPASE: A MINIMAL ALPHA/BETA HYDROLASE ENZYME

Summary for 1I6W

• Entry DOI: 10.2210/pdb1i6w/pdb
• Descriptor: LIPASE A, CADMIUM ION (3 entities in total)
• Functional Keywords: alpha/beta hydrolase, hydrolase
• Biological source: Bacillus subtilis
• Cellular location: Secreted: P37957
• Total number of polymer chains: 2
• Total formula weight: 38878.08

Authors

van Pouderoyen, G.,Eggert, T.,Jaeger, K.-E.,Dijkstra, B.W. (deposition date: 2001-03-05, release date: 2001-05-23, Last modification date: 2024-02-07)

Primary citation

van Pouderoyen, G.,Eggert, T.,Jaeger, K.E.,Dijkstra, B.W.
The crystal structure of Bacillus subtilis lipase: a minimal alpha/beta hydrolase fold enzyme.
J.Mol.Biol., 309:215-226, 2001

PubMed Abstract: The X-ray structure of the lipase LipA from Bacillus subtilis has been determined at 1.5 A resolution. It is the first structure of a member of homology family 1.4 of bacterial lipases. The lipase shows a compact minimal alpha/beta hydrolase fold with a six-stranded parallel beta-sheet flanked by five alpha-helices, two on one side of the sheet and three on the other side. The catalytic triad residues, Ser77, Asp133 and His156, and the residues forming the oxyanion hole (backbone amide groups of Ile12 and Met78) are in positions very similar to those of other lipases of known structure. However, no lid domain is present and the active-site nucleophile Ser77 is solvent-exposed. A model of substrate binding is proposed on the basis of a comparison with other lipases with a covalently bound tetrahedral intermediate mimic. It explains the preference of the enzyme for substrates with C8 fatty acid chains.

PubMed: 11491291
DOI: 10.1006/jmbi.2001.4659

Experimental method

X-RAY DIFFRACTION (1.5 Å)