1gn2

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[[Image:1gn2.jpg|left|200px]]
[[Image:1gn2.jpg|left|200px]]
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{{Structure
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|PDB= 1gn2 |SIZE=350|CAPTION= <scene name='initialview01'>1gn2</scene>, resolution 3.4&Aring;
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The line below this paragraph, containing "STRUCTURE_1gn2", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Catalytic+Site+For+Chain+H'>AC1</scene>
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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=FE:FE+(III)+ION'>FE</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/Superoxide_dismutase Superoxide dismutase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.15.1.1 1.15.1.1] </span>
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{{STRUCTURE_1gn2| PDB=1gn2 | 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=1gn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gn2 OCA], [http://www.ebi.ac.uk/pdbsum/1gn2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gn2 RCSB]</span>
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'''S123C MUTANT OF THE IRON-SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.'''
'''S123C MUTANT OF THE IRON-SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.'''
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[[Category: Tickle, I J.]]
[[Category: Tickle, I J.]]
[[Category: Young, D B.]]
[[Category: Young, D B.]]
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[[Category: iron]]
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[[Category: Iron]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:46:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:47:20 2008''
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Revision as of 14:46, 2 May 2008

Template:STRUCTURE 1gn2

S123C MUTANT OF THE IRON-SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.


Overview

With the aim of enhancing interactions involved in dimer formation, an intersubunit disulfide bridge was engineered in the superoxide dismutase enzyme of Mycobacterium tuberculosis. Ser-123 was chosen for mutation to cysteine since it resides at the dimer interface where the serine side chain interacts with the same residue in the opposite subunit. Gel electrophoresis and X-ray crystallographic studies of the expressed mutant confirmed formation of the disulfide bond under nonreducing conditions. However, the mutant protein was found to be less stable than the wild type as judged by susceptibility to denaturation in the presence of guanidine hydrochloride. Decreased stability probably results from formation of a disulfide bridge with a suboptimal torsion angle and exclusion of solvent molecules from the dimer interface.

About this Structure

1GN2 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

Engineering of an intersubunit disulfide bridge in the iron-superoxide dismutase of Mycobacterium tuberculosis., Bunting KA, Cooper JB, Tickle IJ, Young DB, Arch Biochem Biophys. 2002 Jan 1;397(1):69-76. PMID:11747311 Page seeded by OCA on Fri May 2 17:46:06 2008

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