1gn6

<table><tr><td colspan='2'>[[1gn6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GN6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1GN6 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gn2|1gn2]], [[1gn3|1gn3]], [[1gn4|1gn4]], [[1ids|1ids]]</div></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1gn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gn6 OCA], [http://pdbe.org/1gn6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1gn6 RCSB], [http://www.ebi.ac.uk/pdbsum/1gn6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1gn6 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/SODF_MYCTU SODF_MYCTU]] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:8674528</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Superoxide dismutase]]

[[Category: Badasso, M O]]

[[Category: Bunting, K A]]

[[Category: Cooper, J B]]

[[Category: Erskine, P T]]

[[Category: Saward, S]]

[[Category: Wood, S P]]

[[Category: Young, D B]]

[[Category: Zhang, Y]]

[[Category: Oxidoreductase]]