1gn6

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[[Image:1gn6.jpg|left|200px]]<br /><applet load="1gn6" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1gn6.jpg|left|200px]]<br /><applet load="1gn6" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1gn6, resolution 2.9&Aring;" />
caption="1gn6, resolution 2.9&Aring;" />
'''G152A MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE DISMUTASE.'''<br />
'''G152A MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE DISMUTASE.'''<br />
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==About this Structure==
==About this Structure==
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1GN6 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 FE 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 D'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GN6 OCA].
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1GN6 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+D'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GN6 OCA].
==Reference==
==Reference==
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[[Category: oxidoreductase]]
[[Category: oxidoreductase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:26:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:41:10 2008''

Revision as of 07:41, 3 February 2008


1gn6, resolution 2.9Å

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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, 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.

About this Structure

1GN6 is a Single protein structure of sequence from Mycobacterium tuberculosis with as ligand. Active as Superoxide dismutase, with EC number 1.15.1.1 Known structural/functional Site: . 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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