2klx: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2klx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bartonella_henselae_str._Houston-1 Bartonella henselae str. Houston-1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KLX FirstGlance]. <br> | <table><tr><td colspan='2'>[[2klx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bartonella_henselae_str._Houston-1 Bartonella henselae str. Houston-1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KLX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KLX FirstGlance]. <br> | ||
</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=2klx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2klx OCA], [https://pdbe.org/2klx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2klx RCSB], [https://www.ebi.ac.uk/pdbsum/2klx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2klx ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=2klx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2klx OCA], [https://pdbe.org/2klx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2klx RCSB], [https://www.ebi.ac.uk/pdbsum/2klx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2klx ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
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<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kl/2klx_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kl/2klx_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
Latest revision as of 04:08, 21 November 2024
Solution structure of glutaredoxin from Bartonella henselae str. HoustonSolution structure of glutaredoxin from Bartonella henselae str. Houston
Structural highlights
FunctionA0A0H3LXP0_BARHE Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins.[ARBA:ARBA00002549][RuleBase:RU364065] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedGlutaredoxin proteins (GLXRs) are essential components of the glutathione system that reductively detoxify substances such as arsenic and peroxides and are important in the synthesis of DNA via ribonucleotide reductases. NMR solution structures of glutaredoxin domains from two Gram-negative opportunistic pathogens, Brucella melitensis and Bartonella henselae, are presented. These domains lack the N-terminal helix that is frequently present in eukaryotic GLXRs. The conserved active-site cysteines adopt canonical proline/tyrosine-stabilized geometries. A difference in the angle of alpha-helix 2 relative to the beta-sheet surface and the presence of an extended loop in the human sequence suggests potential regulatory regions and/or protein-protein interaction motifs. This observation is consistent with mutations in this region that suppress defects in GLXR-ribonucleotide reductase interactions. These differences between the human and bacterial forms are adjacent to the dithiol active site and may permit species-selective drug design. Comparative analysis of glutaredoxin domains from bacterial opportunistic pathogens.,Leeper T, Zhang S, Van Voorhis WC, Myler PJ, Varani G Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Sep 1;67(Pt, 9):1141-7. Epub 2011 Aug 16. PMID:21904064[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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