This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1gn6
From Proteopedia
|
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 [Superoxide dismutase], with EC number [1.15.1.1]. Structure known Active Site: AC1. 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
Page seeded by OCA on Tue Oct 30 13:23:06 2007
