1gn6: Difference between revisions

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[[Image:1gn6.jpg|left|200px]]
{{Seed}}
[[Image:1gn6.png|left|200px]]


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{{STRUCTURE_1gn6|  PDB=1gn6  |  SCENE=  }}  
{{STRUCTURE_1gn6|  PDB=1gn6  |  SCENE=  }}  


'''G152A MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE DISMUTASE.'''
===G152A MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE DISMUTASE.===




==Overview==
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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 crystals of this mutant at 2.9 angstroms resolution and subsequent least-squares refinement to an R-value of 0.169 clearly establish that the loop conformation is unaffected. Fluorescence studies of guanidine hydrochloride denaturation establish that the mutant is 4 kcal/mol less stable than the wild-type enzyme. Our results indicate that strict conformational constraints imposed upon a region of polypeptide, due for example to interactions with a neighbouring subunit, may force an alanine residue to adopt this sterically hindered conformation with a consequent reduction in stability of the folded conformation.
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{{ABSTRACT_PUBMED_8674528}}


==About this Structure==
==About this Structure==
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[[Category: Zhang, Y.]]
[[Category: Zhang, Y.]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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