1jea

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[[Image:1jea.jpg|left|200px]]
[[Image:1jea.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1jea |SIZE=350|CAPTION= <scene name='initialview01'>1jea</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1jea", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1jea| PDB=1jea | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jea OCA], [http://www.ebi.ac.uk/pdbsum/1jea PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jea RCSB]</span>
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}}
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'''ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN'''
'''ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN'''
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[[Category: Subtilisin]]
[[Category: Subtilisin]]
[[Category: Bott, R.]]
[[Category: Bott, R.]]
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[[Category: calcium-binding]]
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[[Category: Calcium-binding]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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[[Category: serine protease]]
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[[Category: Serine protease]]
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[[Category: sporulation]]
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[[Category: Sporulation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:07:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:32:25 2008''
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Revision as of 18:07, 2 May 2008

Image:1jea.jpg

Template:STRUCTURE 1jea

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. 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 Page seeded by OCA on Fri May 2 21:07:03 2008

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