1gn2
From Proteopedia
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==Overview== | ==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 . | + | 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== | ==About this Structure== | ||
| - | 1GN2 is a | + | 1GN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis] with FE as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Structure known Active Site: AC1. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GN2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 14:40:26 2007'' |
Revision as of 12:35, 5 November 2007
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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 with FE as ligand. Active as Superoxide dismutase, with EC number 1.15.1.1 Structure known Active Site: AC1. 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 Mon Nov 5 14:40:26 2007
