1gn6
From Proteopedia
(Difference between revisions)
Line 3: | Line 3: | ||
<StructureSection load='1gn6' size='340' side='right'caption='[[1gn6]], [[Resolution|resolution]] 2.90Å' scene=''> | <StructureSection load='1gn6' size='340' side='right'caption='[[1gn6]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[1gn6]] is a 4 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1gn6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycobacterium_tuberculosis Mycobacterium tuberculosis]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1GN6 FirstGlance]. <br> |
- | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> |
- | <tr id=' | + | <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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1gn6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gn6 OCA], [https://pdbe.org/1gn6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gn6 RCSB], [https://www.ebi.ac.uk/pdbsum/1gn6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gn6 ProSAT]</span></td></tr> | |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://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. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 21: | Line 20: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gn6 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1gn6 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1gn6" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | *[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: | + | [[Category: Mycobacterium tuberculosis]] |
- | [[Category: Badasso | + | [[Category: Badasso MO]] |
- | [[Category: Bunting | + | [[Category: Bunting KA]] |
- | [[Category: Cooper | + | [[Category: Cooper JB]] |
- | [[Category: Erskine | + | [[Category: Erskine PT]] |
- | [[Category: Saward | + | [[Category: Saward S]] |
- | [[Category: Wood | + | [[Category: Wood SP]] |
- | [[Category: Young | + | [[Category: Young DB]] |
- | [[Category: Zhang | + | [[Category: Zhang Y]] |
- | + |
Revision as of 11:22, 27 March 2024
G152A mutant of Mycobacterium tuberculosis iron-superoxide dismutase.
|