1de1: Difference between revisions
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==NMR STRUCTURES OF OXIDIZED BACTERIOPHAGE T4 GLUTAREDOXIN== | ==NMR STRUCTURES OF OXIDIZED BACTERIOPHAGE T4 GLUTAREDOXIN== | ||
<StructureSection load='1de1' size='340' side='right' caption='[[1de1 | <StructureSection load='1de1' size='340' side='right'caption='[[1de1]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1de1]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1de1]] 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=1DE1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DE1 FirstGlance]. <br> | ||
</td></tr><tr id=' | </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'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1de1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1de1 OCA], [https://pdbe.org/1de1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1de1 RCSB], [https://www.ebi.ac.uk/pdbsum/1de1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1de1 ProSAT]</span></td></tr> | ||
</table> | </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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/de/1de1_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/de/1de1_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> | ||
</jmolCheckbox> | </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/ | </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=1de1 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Escherichia virus T4]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Amegbey G]] | ||
[[Category: | [[Category: Wang Y]] | ||
[[Category: | [[Category: Wishart DS]] | ||