2tld
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(New page: 200px<br /><applet load="2tld" size="450" color="white" frame="true" align="right" spinBox="true" caption="2tld, resolution 2.6Å" /> '''CRYSTAL STRUCTURE OF ...)
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Revision as of 11:57, 21 November 2007
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CRYSTAL STRUCTURE OF AN ENGINEERED SUBTILISIN INHIBITOR COMPLEXED WITH BOVINE TRYPSIN
Overview
Proteinase specificity of a proteinaceous inhibitor of subtilisin (SSI;, Streptomyces subtilisin inhibitor) can be altered so as to strongly, inhibit trypsin simply by replacing P1 methionine with lysine (with or, without concomitant change of the P4 residue) through site-directed, mutagenesis. Now the crystal structure of one such engineered SSI (P1, methionine converted to lysine and P4 methionine converted to glycine), complexed with bovine trypsin has been solved at 2.6 A resolution and, refined to a crystallographic R factor of 0.173. Comparing this structure, with the previously established structure of the native SSI complexed with, subtilisin BPN', it was found that (i) P1 lysine of the mutant SSI is, accommodated in the S1 pocket of trypsin as usual, and (ii) upon complex, formation, considerable conformation change occurs to the reactive site, loop of the mutant SSI. Thus, in this case, flexibility of the reactive, site loop seems important for successfully changing the proteinase, specificity through mere replacement of the P1 residue.
About this Structure
2TLD is a Protein complex structure of sequences from Bos taurus. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.
Reference
Crystal structure of an engineered subtilisin inhibitor complexed with bovine trypsin., Takeuchi Y, Nonaka T, Nakamura KT, Kojima S, Miura K, Mitsui Y, Proc Natl Acad Sci U S A. 1992 May 15;89(10):4407-11. PMID:1584773
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