4af2: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4af2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AF2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4af2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AF2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AF2 FirstGlance]. <br> | ||
</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=4af2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4af2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4af2 RCSB], [http://www.ebi.ac.uk/pdbsum/4af2 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=4af2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4af2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4af2 RCSB], [http://www.ebi.ac.uk/pdbsum/4af2 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/TPX_ECO57 TPX_ECO57]] Has antioxidant activity. Could remove peroxides or H(2)O(2) within the catalase- and peroxidase-deficient periplasmic space (By similarity). | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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The structure of an orthorhombic crystal form of a `forced reduced' thiol peroxidase reveals lattice formation aided by the presence of the affinity tag.,Beckham KS, Byron O, Roe AJ, Gabrielsen M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 May 1;68(Pt 5):522-6. Epub, 2012 Apr 20. PMID:22691780<ref>PMID:22691780</ref> | The structure of an orthorhombic crystal form of a `forced reduced' thiol peroxidase reveals lattice formation aided by the presence of the affinity tag.,Beckham KS, Byron O, Roe AJ, Gabrielsen M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 May 1;68(Pt 5):522-6. Epub, 2012 Apr 20. PMID:22691780<ref>PMID:22691780</ref> | ||
From | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Beckham, K S.H | [[Category: Beckham, K S.H]] | ||
[[Category: Byron, O | [[Category: Byron, O]] | ||
[[Category: Gabrielsen, M | [[Category: Gabrielsen, M]] | ||
[[Category: Roe, A J | [[Category: Roe, A J]] | ||
[[Category: Inactive mutant]] | [[Category: Inactive mutant]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: Peroxiredoxin]] | [[Category: Peroxiredoxin]] | ||
Revision as of 20:54, 24 December 2014
C61S mutant of thiol peroxidase form E. coli.C61S mutant of thiol peroxidase form E. coli.
Structural highlights
Function[TPX_ECO57] Has antioxidant activity. Could remove peroxides or H(2)O(2) within the catalase- and peroxidase-deficient periplasmic space (By similarity). Publication Abstract from PubMedThiol peroxidase (Tpx) is an atypical 2-Cys peroxiredoxin, which has been suggested to be important for cell survival and virulence in Gram-negative pathogens. The structure of a catalytically inactive version of this protein in an orthorhombic crystal form has been determined by molecular replacement. Structural alignments revealed that Tpx is conserved. Analysis of the crystal packing shows that the linker region of the affinity tag is important for formation of the crystal lattice. The structure of an orthorhombic crystal form of a `forced reduced' thiol peroxidase reveals lattice formation aided by the presence of the affinity tag.,Beckham KS, Byron O, Roe AJ, Gabrielsen M Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 May 1;68(Pt 5):522-6. Epub, 2012 Apr 20. PMID:22691780[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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