1gn6: Difference between revisions
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Revision as of 16:10, 30 October 2007
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G152A MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE DISMUTASE.
OverviewOverview
We have refined the X-ray structure of a site-directed G152A mutant of the, iron-dependent superoxide dismutase from Mycobacterium tuberculosis at 2.9, angstroms resolution. The mutation which replaces a glycine residue in a, surface loop with alanine was designed to alter the conformation of this, loop region which has previously been shown to play a crucial structural, role in quaternary interactions within the SOD tetramer. Gly-152 was, targeted as it has dihedral angles (phi = 83.1 degrees, psi = -0.3, degrees) close to the left-handed alpha-helical conformation which is, rarely adopted by other amino acids except asparagine. Gly-152 was, replaced by alanine as it has similar size and polarity, yet has a very, low tendency to adopt similar conformations. X-ray data collection on, ... [(full description)]
About this StructureAbout this Structure
1GN6 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].
ReferenceReference
X-ray structure analysis of an engineered Fe-superoxide dismutase Gly-Ala mutant with significantly reduced stability to denaturant., Cooper JB, Saward S, Erskine PT, Badasso MO, Wood SP, Zhang Y, Young D, FEBS Lett. 1996 Jun 3;387(2-3):105-8. PMID:8674528
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