2klx
From Proteopedia
(Difference between revisions)
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<StructureSection load='2klx' size='340' side='right' caption='[[2klx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='2klx' size='340' side='right' caption='[[2klx]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | [[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]. <br> | + | <table><tr><td colspan='2'>[[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]. <br> |
| - | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span>< | + | </td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">grxC, BH04010 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=38323 Bartonella henselae])</td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2klx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2klx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2klx RCSB], [http://www.ebi.ac.uk/pdbsum/2klx PDBsum]</span>< | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> |
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2klx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2klx OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2klx RCSB], [http://www.ebi.ac.uk/pdbsum/2klx PDBsum]</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> | ||
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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/chain_selection.php?pdb_ID=2ata 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/chain_selection.php?pdb_ID=2ata 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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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:56, 1 May 2014
Solution structure of glutaredoxin from Bartonella henselae str. Houston
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Categories: Bartonella henselae | Leeper, T C. | SSGCID, Seattle Structural Genomics Center for Infectious Disease. | Varani, G. | Zheng, S. | Electron transport | Glutaredoxin | Oxidoreductase | Seattle structural genomics center for infectious disease | Ssgcid | Structural genomic | Thioredoxin type domain
