2klx

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[[Image:2klx.png|left|200px]]
 
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==Solution structure of glutaredoxin from Bartonella henselae str. Houston==
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The line below this paragraph, containing "STRUCTURE_2klx", creates the "Structure Box" on the page.
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<StructureSection load='2klx' size='340' side='right'caption='[[2klx]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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or leave the SCENE parameter empty for the default display.
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</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>
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<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>
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{{STRUCTURE_2klx| PDB=2klx | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A0H3LXP0_BARHE A0A0H3LXP0_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]
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kl/2klx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2klx ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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===Solution structure of glutaredoxin from Bartonella henselae str. Houston===
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_21904064}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2klx" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 21904064 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21904064}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Bartonella henselae str. Houston-1]]
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[[2klx]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bartonella_henselae Bartonella henselae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KLX OCA].
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[[Category: Large Structures]]
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[[Category: Leeper TC]]
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==Reference==
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[[Category: Varani G]]
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<ref group="xtra">PMID:021904064</ref><references group="xtra"/>
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[[Category: Zheng S]]
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[[Category: Bartonella henselae]]
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[[Category: Leeper, T C.]]
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[[Category: SSGCID, Seattle Structural Genomics Center for Infectious Disease.]]
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[[Category: Varani, G.]]
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[[Category: Zheng, S.]]
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[[Category: Electron transport]]
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[[Category: Glutaredoxin]]
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[[Category: Oxidoreductase]]
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[[Category: Seattle structural genomics center for infectious disease]]
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[[Category: Ssgcid]]
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[[Category: Structural genomic]]
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[[Category: Thioredoxin type domain]]
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Current revision

Solution structure of glutaredoxin from Bartonella henselae str. Houston

PDB ID 2klx

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