1gn2

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[[Image:1gn2.jpg|left|200px]]<br /><applet load="1gn2" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gn2.jpg|left|200px]]
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caption="1gn2, resolution 3.4&Aring;" />
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'''S123C MUTANT OF THE IRON-SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.'''<br />
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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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|SITE= <scene name='pdbsite=AC1:Catalytic+Site+For+Chain+H'>AC1</scene>
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|LIGAND= <scene name='pdbligand=FE:FE (III) ION'>FE</scene>
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|ACTIVITY= [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]
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|GENE=
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}}
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'''S123C MUTANT OF THE IRON-SUPEROXIDE DISMUTASE FROM MYCOBACTERIUM TUBERCULOSIS.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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 <scene name='pdbligand=FE:'>FE</scene> 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] Known structural/functional Site: <scene name='pdbsite=AC1:Catalytic+Site+For+Chain+H'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GN2 OCA].
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1GN2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GN2 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11747311 11747311]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11747311 11747311]
[[Category: Mycobacterium tuberculosis]]
[[Category: Mycobacterium tuberculosis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:25:18 2008''

Revision as of 09:25, 20 March 2008


PDB ID 1gn2

Drag the structure with the mouse to rotate
, resolution 3.4Å
Sites:
Ligands:
Activity: Superoxide dismutase, with EC number 1.15.1.1
Coordinates: save as pdb, mmCIF, xml



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

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