1qk8: Difference between revisions
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==TRYPAREDOXIN-I FROM CRITHIDIA FASCICULATA== | ==TRYPAREDOXIN-I FROM CRITHIDIA FASCICULATA== | ||
<StructureSection load='1qk8' size='340' side='right' caption='[[1qk8]], [[Resolution|resolution]] 1.40Å' scene=''> | <StructureSection load='1qk8' size='340' side='right' caption='[[1qk8]], [[Resolution|resolution]] 1.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1qk8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Crifa Crifa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QK8 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1qk8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Crifa Crifa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QK8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QK8 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qk8 OCA], [http://pdbe.org/1qk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qk8 RCSB], [http://www.ebi.ac.uk/pdbsum/1qk8 PDBsum]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qk8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qk8 OCA], [http://pdbe.org/1qk8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qk8 RCSB], [http://www.ebi.ac.uk/pdbsum/1qk8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qk8 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qk/1qk8_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qk/1qk8_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> | ||
Revision as of 11:09, 24 February 2018
TRYPAREDOXIN-I FROM CRITHIDIA FASCICULATATRYPAREDOXIN-I FROM CRITHIDIA FASCICULATA
Structural highlights
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 PubMedTryparedoxin-I is a recently discovered thiol-disulfide oxidoreductase involved in the regulation of oxidative stress in parasitic trypanosomatids. The crystal structure of recombinant Crithidia fasciculata tryparedoxin-I in the oxidized state has been determined using multi-wavelength anomalous dispersion methods applied to a selenomethionyl derivative. The model comprises residues 3 to 145 with 236 water molecules and has been refined using all data between a 19- and 1.4-A resolution to an R-factor and R-free of 19.1 and 22.3%, respectively. Despite sharing only about 20% sequence identity, tryparedoxin-I presents a five-stranded twisted beta-sheet and two elements of helical structure in the same type of fold as displayed by thioredoxin, the archetypal thiol-disulfide oxidoreductase. However, the relationship of secondary structure with the linear amino acid sequences is different for each protein, producing a distinctive topology. The beta-sheet core is extended in the trypanosomatid protein with an N-terminal beta-hairpin. There are also differences in the content and orientation of helical elements of secondary structure positioned at the surface of the proteins, which leads to different shapes and charge distributions between human thioredoxin and tryparedoxin-I. A right-handed redox-active disulfide is formed between Cys-40 and Cys-43 at the N-terminal region of a distorted alpha-helix (alpha1). Cys-40 is solvent-accessible, and Cys-43 is positioned in a hydrophilic cavity. Three C-H...O hydrogen bonds donated from two proline residues serve to stabilize the disulfide-carrying helix and support the correct alignment of active site residues. The accurate model for tryparedoxin-I allows for comparisons with the family of thiol-disulfide oxidoreductases and provides a template for the discovery or design of selective inhibitors of hydroperoxide metabolism in trypanosomes. Such inhibitors are sought as potential therapies against a range of human pathogens. The high resolution crystal structure of recombinant Crithidia fasciculata tryparedoxin-I.,Alphey MS, Leonard GA, Gourley DG, Tetaud E, Fairlamb AH, Hunter WN J Biol Chem. 1999 Sep 3;274(36):25613-22. PMID:10464297[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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