4af2: Difference between revisions
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New page: '''Unreleased structure''' The entry 4af2 is ON HOLD until Paper Publication Authors: Beckham, K.S.H., Roe, A.J., Byron, O., Gabrielsen, M. Description: C61S mutant of thiol peroxidase... |
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==C61S mutant of thiol peroxidase form E. coli.== | |||
<StructureSection load='4af2' size='340' side='right'caption='[[4af2]], [[Resolution|resolution]] 1.97Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4af2]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4AF2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.97Å</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=4af2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4af2 OCA], [https://pdbe.org/4af2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4af2 RCSB], [https://www.ebi.ac.uk/pdbsum/4af2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4af2 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/TPX_ECOLI TPX_ECOLI] Has antioxidant activity. Could remove peroxides or H(2)O(2) within the catalase- and peroxidase-deficient periplasmic space.[HAMAP-Rule:MF_00269] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Thiol 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<ref>PMID:22691780</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4af2" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Thiol peroxidase 3D structures|Thiol peroxidase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | |||
[[Category: Large Structures]] | |||
[[Category: Beckham KSH]] | |||
[[Category: Byron O]] | |||
[[Category: Gabrielsen M]] | |||
[[Category: Roe AJ]] | |||
Latest revision as of 14:25, 20 December 2023
C61S mutant of thiol peroxidase form E. coli.C61S mutant of thiol peroxidase form E. coli.
Structural highlights
FunctionTPX_ECOLI Has antioxidant activity. Could remove peroxides or H(2)O(2) within the catalase- and peroxidase-deficient periplasmic space.[HAMAP-Rule:MF_00269] 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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