3ot7: Difference between revisions
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New page: '''Unreleased structure''' The entry 3ot7 is ON HOLD until Paper Publication Authors: Whittaker, M.M., Lerch, T.F., Kirillova, O., Chapman, M.S., Whittaker, J.W. Description: Escherich... |
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==Escherichia coli apo-manganese superoxide dismutase== | |||
<StructureSection load='3ot7' size='340' side='right'caption='[[3ot7]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ot7]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OT7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OT7 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.901Å</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=3ot7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ot7 OCA], [https://pdbe.org/3ot7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ot7 RCSB], [https://www.ebi.ac.uk/pdbsum/3ot7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ot7 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SODM_ECOLI SODM_ECOLI] Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Metal binding by apo-manganese superoxide dismutase (apo-MnSOD) is essential for functional maturation of the enzyme. Previous studies have demonstrated that metal binding by apo-MnSOD is conformationally gated, requiring protein reorganization for the metal to bind. We have now solved the X-ray crystal structure of apo-MnSOD at 1.9A resolution. The organization of active site residues is independent of the presence of the metal cofactor, demonstrating that protein itself templates the unusual metal coordination geometry. Electrophoretic analysis of mixtures of apo- and (Mn(2))-MnSOD, dye-conjugated protein, or C-terminal Strep-tag II fusion protein reveals a dynamic subunit exchange process associated with cooperative metal binding by the two subunits of the dimeric protein. In contrast, (S126C) (SS) apo-MnSOD, which contains an inter-subunit covalent disulfide-crosslink, exhibits anti-cooperative metal binding. The protein concentration dependence of metal uptake kinetics implies that protein dissociation is involved in metal binding by the wild type apo-protein, although other processes may also contribute to gating metal uptake. Protein concentration dependent small-zone size exclusion chromatography is consistent with apo-MnSOD dimer dissociation at low protein concentration (K(D)=1x10(-6)M). Studies on metal uptake by apo-MnSOD in Escherichia coli cells show that the protein exhibits similar behavior in vivo and in vitro. | |||
Subunit dissociation and metal binding by Escherichia coli apo-manganese superoxide dismutase.,Whittaker MM, Lerch TF, Kirillova O, Chapman MS, Whittaker JW Arch Biochem Biophys. 2010 Oct 31. PMID:21044611<ref>PMID:21044611</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3ot7" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Superoxide dismutase 3D structures|Superoxide dismutase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Chapman MS]] | |||
[[Category: Kirillova O]] | |||
[[Category: Lerch TF]] | |||
[[Category: Whittaker JW]] | |||
[[Category: Whittaker MM]] | |||
Latest revision as of 09:44, 6 September 2023
Escherichia coli apo-manganese superoxide dismutase
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