1ags

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[[Image:1ags.gif|left|200px]]
[[Image:1ags.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1ags |SIZE=350|CAPTION= <scene name='initialview01'>1ags</scene>, resolution 2.5&Aring;
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The line below this paragraph, containing "STRUCTURE_1ags", 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=GTX:S-HEXYLGLUTATHIONE'>GTX</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/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= PGTH121-G82R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=32630 synthetic construct])
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-->
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|DOMAIN=
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{{STRUCTURE_1ags| PDB=1ags | 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=1ags FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ags OCA], [http://www.ebi.ac.uk/pdbsum/1ags PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ags RCSB]</span>
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}}
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'''A SURFACE MUTANT (G82R) OF A HUMAN ALPHA-GLUTATHIONE S-TRANSFERASE SHOWS DECREASED THERMAL STABILITY AND A NEW MODE OF MOLECULAR ASSOCIATION IN THE CRYSTAL'''
'''A SURFACE MUTANT (G82R) OF A HUMAN ALPHA-GLUTATHIONE S-TRANSFERASE SHOWS DECREASED THERMAL STABILITY AND A NEW MODE OF MOLECULAR ASSOCIATION IN THE CRYSTAL'''
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[[Category: Wang, B C.]]
[[Category: Wang, B C.]]
[[Category: Zeng, K.]]
[[Category: Zeng, K.]]
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[[Category: transferase (glutathione)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:15:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:39:53 2008''
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Revision as of 07:15, 2 May 2008

Image:1ags.gif

Template:STRUCTURE 1ags

A SURFACE MUTANT (G82R) OF A HUMAN ALPHA-GLUTATHIONE S-TRANSFERASE SHOWS DECREASED THERMAL STABILITY AND A NEW MODE OF MOLECULAR ASSOCIATION IN THE CRYSTAL


Overview

A chimeric enzyme (GST121) of the human alpha-glutathione S-transferases GST1-1 and GST2-2, which has improved catalytic efficiency and thermostability from its wild-type parent proteins, has been crystallized in a space group that is isomorphous with that reported for crystals of GST1-1. However, a single-site (G82R) mutant of GST121, which exhibits a significant reduction both in vitro and in vivo in protein thermostability, forms crystals that are not isomorphous with GST1-1. The mutant protein crystallizes in space group P2(1)2(1)2(1), with cell dimensions a = 49.5, b = 92.9, c = 115.9 A, and one dimer per asymmetric unit. Preliminary crystallographic results show that a mutation of the surface residue Gly 82 from a neutral to a charged residue causes new salt bridges to be formed among the GST dimers, suggesting that the G82R mutant might aggregate more readily than does GST121 in solution, resulting in a change of its solution properties.

About this Structure

1AGS is a Single protein structure of sequence from Synthetic construct. Full crystallographic information is available from OCA.

Reference

A surface mutant (G82R) of a human alpha-glutathione S-transferase shows decreased thermal stability and a new mode of molecular association in the crystal., Zeng K, Rose JP, Chen HC, Strickland CL, Tu CP, Wang BC, Proteins. 1994 Nov;20(3):259-63. PMID:7892174 Page seeded by OCA on Fri May 2 10:15:01 2008

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