1gn2

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{{STRUCTURE_1gn2| PDB=1gn2 | SCENE= }}
{{STRUCTURE_1gn2| PDB=1gn2 | SCENE= }}
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'''S123C MUTANT OF THE IRON-SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.'''
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===S123C MUTANT OF THE IRON-SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11747311 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11747311}}
==About this Structure==
==About this Structure==
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[[Category: Iron]]
[[Category: Iron]]
[[Category: Oxidoreductase]]
[[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 Tue Jul 1 05:32:22 2008''

Revision as of 02:32, 1 July 2008

Image:1gn2.png

Template:STRUCTURE 1gn2

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

Template:ABSTRACT PUBMED 11747311

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

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