1c9j: Difference between revisions

Revision as of 20:24, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1c9j.png

Template:STRUCTURE 1c9j

BACILLUS LENTUS SUBTILISIN K27R/N87S/V104Y/N123S/T274A VARIANTBACILLUS LENTUS SUBTILISIN K27R/N87S/V104Y/N123S/T274A VARIANT

Template:ABSTRACT PUBMED 10493860

About this StructureAbout this Structure

1C9J is a Single protein structure of sequence from Bacillus lentus. Full crystallographic information is available from OCA.

ReferenceReference

Engineered Bacillus lentus subtilisins having altered flexibility., Graycar T, Knapp M, Ganshaw G, Dauberman J, Bott R, J Mol Biol. 1999 Sep 10;292(1):97-109. PMID:10493860

Page seeded by OCA on Mon Jun 30 20:24:30 2008

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 {{STRUCTURE_1c9j|  PDB=1c9j  |  SCENE=  }}
-'''BACILLUS LENTUS SUBTILISIN K27R/N87S/V104Y/N123S/T274A VARIANT'''
+===BACILLUS LENTUS SUBTILISIN K27R/N87S/V104Y/N123S/T274A VARIANT===
-==Overview==
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-The three-dimensional structures of engineered variants of Bacillus lentus subtilisin having increased enzymatic activity, K27R/N87S/V104Y/N123S/T274A (RSYSA) and N76D/N87S/S103A/V104I (DSAI), were determined by X-ray crystallography. In addition to identifying changes in atomic position we report a method that identifies protein segments having altered flexibility. The method utilizes a statistical analysis of variance to delineate main-chain temperature factors that represent significant departures from the overall variance between equivalent regions seen throughout the structure. This method reveals changes in main-chain mobility in both variants. Residues 125-127 have increased mobility in the RSYSA variant while residues 100-104 have decreased mobility in the DSAI variant. These segments are located at the substrate-binding site and changes in their mobility are believed to relate to the observed changes in proteolytic activity. The effect of altered crystal lattice contacts on segment flexibility becomes apparent when identical variants, determined in two crystal forms, are compared with the native enzyme.
+The line below this paragraph, {{ABSTRACT_PUBMED_10493860}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10493860 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10493860}}
 ==About this Structure==
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 [[Category: Hydrolase]]
 [[Category: Subtilisin]]
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