1jea

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(New page: 200px<br /><applet load="1jea" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jea, resolution 2.0&Aring;" /> '''ALTERED TOPOLOGY AND ...)
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'''ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN'''<br />
'''ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN'''<br />
==Overview==
==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.
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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.
==About this Structure==
==About this Structure==
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1JEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_lentus Bacillus lentus] with CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JEA OCA].
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1JEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_lentus Bacillus lentus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEA OCA].
==Reference==
==Reference==
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[[Category: sporulation]]
[[Category: sporulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:09:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:38 2008''

Revision as of 11:21, 21 February 2008

Image:1jea.jpg

1jea, resolution 2.0Å

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ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN

Overview

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.

About this Structure

1JEA is a Single protein structure of sequence from Bacillus lentus with and as ligands. Active as Subtilisin, with EC number 3.4.21.62 Full crystallographic information is available from OCA.

Reference

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

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