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2khp
From Proteopedia
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==Solution structure of Glutaredoxin from Brucella melitensis== | ==Solution structure of Glutaredoxin from Brucella melitensis== | ||
| - | <StructureSection load='2khp' size='340' side='right' caption='[[2khp]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2khp' size='340' side='right'caption='[[2khp]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | [[2khp]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2khp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"micrococcus_melitensis"_(hughes_1893)_bruce_1893 "micrococcus melitensis" (hughes 1893) bruce 1893]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KHP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KHP FirstGlance]. <br> |
| - | <b> | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BMEI0184 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29459 "Micrococcus melitensis" (Hughes 1893) Bruce 1893])</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=2khp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2khp OCA], [https://pdbe.org/2khp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2khp RCSB], [https://www.ebi.ac.uk/pdbsum/2khp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2khp ProSAT]</span></td></tr> | ||
| + | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| - | [[Image:Consurf_key_small.gif|right]] | + | [[Image:Consurf_key_small.gif|200px|right]] |
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kh/2khp_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kh/2khp_consurf.spt"</scriptWhenChecked> |
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| - | </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/ | + | </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=2khp ConSurf]. |
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Glutaredoxin 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. | Glutaredoxin 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. | ||
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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<ref>PMID:21904064</ref> | 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<ref>PMID:21904064</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> | ||
| + | <div class="pdbe-citations 2khp" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Leeper, T | + | [[Category: Leeper, T]] |
| - | [[Category: | + | [[Category: Structural genomic]] |
| - | [[Category: Varani, G | + | [[Category: Varani, G]] |
| - | [[Category: Zheng, S | + | [[Category: Zheng, S]] |
[[Category: Electron transport]] | [[Category: Electron transport]] | ||
[[Category: Glutaredoxin]] | [[Category: Glutaredoxin]] | ||
| - | [[Category: Seattle structural genomics center for infectious disease]] | ||
[[Category: Ssgcid]] | [[Category: Ssgcid]] | ||
| - | [[Category: Structural genomic]] | ||
[[Category: Thioredoxin type domain]] | [[Category: Thioredoxin type domain]] | ||
Current revision
Solution structure of Glutaredoxin from Brucella melitensis
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