1ea7: Difference between revisions
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[[Category: subtilisin like protease]] | [[Category: subtilisin like protease]] | ||
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Revision as of 16:04, 30 October 2007
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SPHERICASE
OverviewOverview
We have previously isolated sphericase (Sph), an extracellular mesophilic, serine protease produced by Bacillus sphaericus. The Sph amino acid, sequence is highly homologous to two cold-adapted subtilisins from, Antarctic bacilli S39 and S41 (76% and 74% identity, respectively). Sph is, calcium-dependent, 310 amino acid residues long and has optimal activity, at pH 10.0. S41 and S39 have not as yet been structurally analysed.In the, present work, we determined the crystal structure of Sph by the, Eu/multiwavelength anomalous diffraction method. The structure was, extended to 0.93A resolution and refined to a crystallographic R-factor of, 9.7%. The final model included all 310 amino acid residues, one disulfide, bond, 679 water molecules and five calcium ions. Although Sph is a, mesophilic ... [(full description)]
About this StructureAbout this Structure
1EA7 is a [Single protein] structure of sequence from [Lysinibacillus sphaericus] with CA and S as [ligands]. Structure known Active Site: 1. Full crystallographic information is available from [OCA].
ReferenceReference
The 0.93A crystal structure of sphericase: a calcium-loaded serine protease from Bacillus sphaericus., Almog O, Gonzalez A, Klein D, Greenblatt HM, Braun S, Shoham G, J Mol Biol. 2003 Oct 3;332(5):1071-82. PMID:14499610
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