1gn6

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[[Image:1gn6.jpg|left|200px]]
[[Image:1gn6.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1gn6 |SIZE=350|CAPTION= <scene name='initialview01'>1gn6</scene>, resolution 2.9&Aring;
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The line below this paragraph, containing "STRUCTURE_1gn6", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Catalytic+Site+For+Chain+D'>AC1</scene>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE=
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|DOMAIN=
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{{STRUCTURE_1gn6| PDB=1gn6 | SCENE= }}
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gn6 OCA], [http://www.ebi.ac.uk/pdbsum/1gn6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gn6 RCSB]</span>
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}}
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'''G152A MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE DISMUTASE.'''
'''G152A MUTANT OF MYCOBACTERIUM TUBERCULOSIS IRON-SUPEROXIDE DISMUTASE.'''
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[[Category: Young, D B.]]
[[Category: Young, D B.]]
[[Category: Zhang, Y.]]
[[Category: Zhang, Y.]]
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[[Category: oxidoreductase]]
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[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:46:14 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:47:24 2008''
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Revision as of 14:46, 2 May 2008

Image:1gn6.jpg

Template:STRUCTURE 1gn6

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. 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 Fri May 2 17:46:14 2008

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