1gn6
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(New page: 200px<br /> <applet load="1gn6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gn6, resolution 2.9Å" /> '''G152A MUTANT OF MYCO...)
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Revision as of 18:27, 29 October 2007
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G152A MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE DISMUTASE.
Overview
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 Structure
1GN6 is a [Single protein] structure of sequence from [Mycobacterium tuberculosis] with FE as [ligand]. Active as [[1]], with EC number [1.15.1.1]. Full crystallographic information is available from [OCA].
Reference
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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