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1grx

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(New page: 200px<br /><applet load="1grx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1grx" /> '''STRUCTURE OF E. COLI GLUTAREDOXIN'''<br /> ...)
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[[Image:1grx.gif|left|200px]]<br /><applet load="1grx" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1grx" />
 
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'''STRUCTURE OF E. COLI GLUTAREDOXIN'''<br />
 
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==Overview==
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==STRUCTURE OF E. COLI GLUTAREDOXIN==
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The determination of the NMR structure of oxidized Escherichia coli, glutaredoxin in aqueous solution is described, and comparisons of this, structure with that of reduced E. coli glutaredoxin and the related, proteins E. coli thioredoxin and T4 glutaredoxin are presented. Based on, nearly complete sequence-specific 1H-NMR assignments, 804 nuclear, Overhauser enhancement distance constraints and 74 dihedral angle, constraints were obtained as the input for the structure calculations, for, which the distance geometry program DIANA was used followed by simulated, annealing with the program X-PLOR. The molecular architecture of oxidized, glutaredoxin is made up of three helices and a four-stranded beta-sheet., The three-dimensional structures of oxidized and the recently described, reduced glutaredoxin are very similar. Quantitative analysis of the, exchange rates of 34 slowly exchanging amide protons from corresponding, series of two-dimensional [15N,1H]-correlated spectra of oxidized and, reduced glutaredoxin showed close agreement, indicating almost identical, hydrogen-bonding patterns. Nonetheless, differences in local dynamics, involving residues near the active site and the C-terminal alpha-helix, were clearly manifested. Comparison of the structure of E. coli, glutaredoxin with those of T4 glutaredoxin and E. coli thioredoxin showed, that all three proteins have a similar overall polypeptide fold. An area, of the protein surface at the active site containing Arg 8, Cys 11, Pro, 12, Tyr 13, Ile 38, Thr 58, Val 59, Pro 60, Gly 71, Tyr 72, and Thr 73 is, proposed as a possible site for interaction with other proteins, in, particular ribonucleotide reductase. It was found that this area, corresponds to previously proposed interaction sites in T4 glutaredoxin, and E. coli thioredoxin. The solvent-accessible surface area at the active, site of E. coli glutaredoxin showed a general trend to increase upon, reduction. Only the sulfhydryl group of Cys 11 is exposed to the solvent, whereas that of Cys 14 is buried and solvent inaccessible.
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<StructureSection load='1grx' size='340' side='right'caption='[[1grx]]' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1grx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GRX FirstGlance]. <br>
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1GRX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with GTT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GRX OCA].
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=GSH:GLUTATHIONE'>GSH</scene></td></tr>
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==Reference==
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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=1grx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1grx OCA], [https://pdbe.org/1grx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1grx RCSB], [https://www.ebi.ac.uk/pdbsum/1grx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1grx ProSAT]</span></td></tr>
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NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins., Xia TH, Bushweller JH, Sodano P, Billeter M, Bjornberg O, Holmgren A, Wuthrich K, Protein Sci. 1992 Mar;1(3):310-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1304339 1304339]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GLRX1_ECOLI GLRX1_ECOLI] The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing some disulfide bonds in a coupled system with glutathione reductase.
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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/gr/1grx_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1grx ConSurf].
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Billeter, M.]]
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[[Category: Billeter M]]
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[[Category: Bushweller, J.H.]]
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[[Category: Bushweller JH]]
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[[Category: Holmgren, L.A.]]
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[[Category: Holmgren LA]]
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[[Category: Wuthrich, K.]]
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[[Category: Wuthrich K]]
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[[Category: GTT]]
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[[Category: electron transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:15:34 2007''
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Current revision

STRUCTURE OF E. COLI GLUTAREDOXIN

PDB ID 1grx

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