1c9j: Difference between revisions
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'''BACILLUS LENTUS SUBTILISIN K27R/N87S/V104Y/N123S/T274A VARIANT''' | {{Structure | ||
|PDB= 1c9j |SIZE=350|CAPTION= <scene name='initialview01'>1c9j</scene>, resolution 1.8Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''BACILLUS LENTUS SUBTILISIN K27R/N87S/V104Y/N123S/T274A VARIANT''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1C9J is a [ | 1C9J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_lentus Bacillus lentus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C9J OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/10493860 10493860] | ||
[[Category: Bacillus lentus]] | [[Category: Bacillus lentus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: subtilisin]] | [[Category: subtilisin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:21:35 2008'' | ||
Revision as of 11:21, 20 March 2008
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| , resolution 1.8Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Subtilisin, with EC number 3.4.21.62 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
BACILLUS LENTUS SUBTILISIN K27R/N87S/V104Y/N123S/T274A VARIANT
OverviewOverview
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 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
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