1s02

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[[Image:1s02.gif|left|200px]]
[[Image:1s02.gif|left|200px]]
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{{Structure
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|PDB= 1s02 |SIZE=350|CAPTION= <scene name='initialview01'>1s02</scene>, resolution 1.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1s02", 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_1s02| PDB=1s02 | 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=1s02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s02 OCA], [http://www.ebi.ac.uk/pdbsum/1s02 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1s02 RCSB]</span>
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}}
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'''EFFECTS OF ENGINEERED SALT BRIDGES ON THE STABILITY OF SUBTILISIN BPN''''
'''EFFECTS OF ENGINEERED SALT BRIDGES ON THE STABILITY OF SUBTILISIN BPN''''
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[[Category: Oliver, J D.]]
[[Category: Oliver, J D.]]
[[Category: Sullivan, J F.]]
[[Category: Sullivan, J F.]]
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[[Category: hydrolase (serine proteinase)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:07:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:35:27 2008''
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Revision as of 05:07, 3 May 2008

Image:1s02.gif

Template:STRUCTURE 1s02

EFFECTS OF ENGINEERED SALT BRIDGES ON THE STABILITY OF SUBTILISIN BPN'


Overview

Variants designed using PROTEUS have been produced in an attempt to engineer stabilizing salt bridges into subtilisin BPN'. All the mutants constructed by site-directed mutagenesis were secreted by Bacillus subtilis, except L75K. Q19E, expressed as a single variant and also in a double variant, Q19E/Q271E, appears to form a stabilizing salt bridge based on X-ray crystal structure determination and differential scanning calorimeter measurements. Although the double mutant was found to be less thermodynamically stable than the wild-type, it did exhibit an autolytic stability about two-fold greater under hydrophobic conditions. Four variants, A98K, S89E, V26R and L235R, were found to be nearly identical to wild-type in thermal stability, indicative of stable structures without evidence of salt bridge formation. Variants Q271E, V51K and T164R led to structures that resulted in varying degrees of thermodynamic and autolytic instability. A computer-modeling analysis of the PROTEUS predictions reveals that the low percentage of salt bridge formation is probably due to an overly simplistic electrostatic model, which does not account for the geometry of the pairwise interactions.

About this Structure

1S02 is a Single protein structure of sequence from Bacillus amyloliquefaciens. Full crystallographic information is available from OCA.

Reference

Effects of engineered salt bridges on the stability of subtilisin BPN'., Erwin CR, Barnett BL, Oliver JD, Sullivan JF, Protein Eng. 1990 Oct;4(1):87-97. PMID:2127106 Page seeded by OCA on Sat May 3 08:07:43 2008

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