1aaz

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[[Image:1aaz.png|left|200px]]
 
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==THE STRUCTURE OF OXIDIZED BACTERIOPHAGE T4 GLUTAREDOXIN (THIOREDOXIN)==
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The line below this paragraph, containing "STRUCTURE_1aaz", creates the "Structure Box" on the page.
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<StructureSection load='1aaz' size='340' side='right'caption='[[1aaz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1aaz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AAZ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
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{{STRUCTURE_1aaz| PDB=1aaz | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aaz OCA], [https://pdbe.org/1aaz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aaz RCSB], [https://www.ebi.ac.uk/pdbsum/1aaz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aaz ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aa/1aaz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1aaz ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The structure of wild-type bacteriophage T4 glutaredoxin (earlier called thioredoxin) in its oxidized form has been refined in a monoclinic crystal form at 2.0 A resolution to a crystallographic R-factor of 0.209. A mutant T4 glutaredoxin gives orthorhombic crystals of better quality. The structure of this mutant has been solved by molecular replacement methods and refined at 1.45 A to an R-value of 0.175. In this mutant glutaredoxin, the active site residues Val15 and Tyr16 have been substituted by Gly and Pro, respectively, to mimic that of Escherichia coli thioredoxin. The main-chain conformation of the wild-type protein is similar in the two independently determined molecules in the asymmetric unit of the monoclinic crystals. On the other hand, side-chain conformations differ considerably between the two molecules due to heterologous packing interactions in the crystals. The structure of the mutant protein is very similar to the wild-type protein, except at mutated positions and at parts involved in crystal contacts. The active site disulfide bridge between Cys14 and Cys17 is located at the first turn of helix alpha 1. The torsion angles of these residues are similar to those of Escherichia coli thioredoxin. The torsion angle around the S-S bond is smaller than that normally observed for disulfides: 58 degrees, 67 degrees and 67 degrees for wild-type glutaredoxin molecule A and B and mutant glutaredoxin, respectively. Each sulfur atom of the disulfide cysteines in T4 glutaredoxin forms a hydrogen bond to one main-chain nitrogen atom. The active site is shielded from solvent on one side by the beta-carbon atoms of the cysteine residues plus side-chains of residues 7, 9, 21 and 33. From the opposite side, there is a cleft where the sulfur atom of Cys14 is accessible and can be attacked by a nucleophilic thiolate ion in the initial step of the reduction reaction.
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===THE STRUCTURE OF OXIDIZED BACTERIOPHAGE T4 GLUTAREDOXIN (THIOREDOXIN)===
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Structure of oxidized bacteriophage T4 glutaredoxin (thioredoxin). Refinement of native and mutant proteins.,Eklund H, Ingelman M, Soderberg BO, Uhlin T, Nordlund P, Nikkola M, Sonnerstam U, Joelson T, Petratos K J Mol Biol. 1992 Nov 20;228(2):596-618. PMID:1453466<ref>PMID:1453466</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_1453466}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1aaz" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 1453466 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_1453466}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Escherichia virus T4]]
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[[1aaz]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AAZ OCA].
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[[Category: Large Structures]]
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[[Category: Eklund H]]
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==Reference==
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[[Category: Ingelman M]]
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<ref group="xtra">PMID:001453466</ref><ref group="xtra">PMID:009099998</ref><references group="xtra"/>
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[[Category: Joelson T]]
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[[Category: Enterobacteria phage t4]]
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[[Category: Nikkola M]]
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[[Category: Eklund, H.]]
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[[Category: Nordlund P]]
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[[Category: Ingelman, M.]]
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[[Category: Petratos K]]
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[[Category: Joelson, T.]]
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[[Category: Soderberg B-O]]
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[[Category: Nikkola, M.]]
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[[Category: Sonnerstam U]]
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[[Category: Nordlund, P.]]
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[[Category: Uhlin T]]
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[[Category: Petratos, K.]]
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[[Category: Soderberg, B O.]]
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[[Category: Sonnerstam, U.]]
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[[Category: Uhlin, T.]]
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[[Category: Electron transport]]
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Current revision

THE STRUCTURE OF OXIDIZED BACTERIOPHAGE T4 GLUTAREDOXIN (THIOREDOXIN)

PDB ID 1aaz

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