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1isp

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{{STRUCTURE_1isp| PDB=1isp | SCENE= }}
{{STRUCTURE_1isp| PDB=1isp | SCENE= }}
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'''Crystal structure of Bacillus subtilis lipase at 1.3A resolution'''
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===Crystal structure of Bacillus subtilis lipase at 1.3A resolution===
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==Overview==
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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 et al. (2001). J. Mol. Biol. 309, 215-226]. In the present study, a new crystal form of BsL which provides diffraction data to higher resolution was obtained and its structure was determined at 1.3 A using the MAD method. It was found that the active-site residue Ser77 has alternate side-chain conformations. The O(gamma) atom of the first conformer forms a hydrogen bond to the N(epsilon) atom of His155, a member of the catalytic triad. In contrast, the second conformer is constructed with a hydrogen bond to the side-chain atom of the adjacent His76. These two conformers presumably correspond to the active and inactive states, respectively. Similar alternate conformations in the catalytic serine residue have been observed in Fusarium solani cutinase determined at 1.0 A resolution and Penicillium purpurogenum acetylxylan esterase at 0.9 A resolution. In addition, a glycerol molecule, which was used as a cryoprotectant, is found to be located in the active site. On the basis of these results, a model for substrate binding in the reaction-intermediate state of BsL is proposed.
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(as it appears on PubMed at http://www.pubmed.gov), where 12077437 is the PubMed ID number.
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{{ABSTRACT_PUBMED_12077437}}
==About this Structure==
==About this Structure==
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[[Category: Tsuda, S.]]
[[Category: Tsuda, S.]]
[[Category: Alpha/beta hydrolase fold]]
[[Category: Alpha/beta hydrolase fold]]
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Revision as of 10:56, 1 July 2008

Image:1isp.png

Template:STRUCTURE 1isp

Crystal structure of Bacillus subtilis lipase at 1.3A resolution

Template:ABSTRACT PUBMED 12077437

About this Structure

1ISP is a Single protein structure of sequence from Bacillus subtilis. Full crystallographic information is available from OCA.

Reference

Alternate conformations observed in catalytic serine of Bacillus subtilis lipase determined at 1.3 A resolution., Kawasaki K, Kondo H, Suzuki M, Ohgiya S, Tsuda S, Acta Crystallogr D Biol Crystallogr. 2002 Jul;58(Pt 7):1168-74. Epub 2002, Jun 20. PMID:12077437

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