1de2: Difference between revisions
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==NMR STRUCTURES OF REDUCED BACTERIOPHAGE T4 GLUTAREDOXIN== | |||
<StructureSection load='1de2' size='340' side='right'caption='[[1de2]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1de2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DE2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DE2 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1de2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1de2 OCA], [https://pdbe.org/1de2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1de2 RCSB], [https://www.ebi.ac.uk/pdbsum/1de2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1de2 ProSAT]</span></td></tr> | ||
[[1de2]] is a 1 chain structure with sequence from [ | </table> | ||
== Function == | |||
== | [https://www.uniprot.org/uniprot/GLRX_BPT4 GLRX_BPT4] Serves as a reducing agent for the phage-induced ribonucleotide reductase, but not for the bacterial ones. This specificity may be the result of sequence differences around the redox-active disulfide bond. The oxidized form accepts electrons from bacterial glutathione and will, in turn, reduce other small disulfides. Can also be reduced by NADPH and by bacterial thioredoxin reductase.<ref>PMID:8440680</ref> | ||
< | == Evolutionary Conservation == | ||
[[ | [[Image:Consurf_key_small.gif|200px|right]] | ||
[[Category: | Check<jmol> | ||
[[Category: | <jmolCheckbox> | ||
[[Category: | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/de/1de2_consurf.spt"</scriptWhenChecked> | ||
[[Category: | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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=1de2 ConSurf]. | |||
<div style="clear:both"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia virus T4]] | |||
[[Category: Large Structures]] | |||
[[Category: Wang Y]] | |||
[[Category: Wishart DS]] | |||
Latest revision as of 12:49, 20 March 2024
NMR STRUCTURES OF REDUCED BACTERIOPHAGE T4 GLUTAREDOXINNMR STRUCTURES OF REDUCED BACTERIOPHAGE T4 GLUTAREDOXIN
Structural highlights
FunctionGLRX_BPT4 Serves as a reducing agent for the phage-induced ribonucleotide reductase, but not for the bacterial ones. This specificity may be the result of sequence differences around the redox-active disulfide bond. The oxidized form accepts electrons from bacterial glutathione and will, in turn, reduce other small disulfides. Can also be reduced by NADPH and by bacterial thioredoxin reductase.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. References |
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