1egr

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{{Seed}}
 
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[[Image:1egr.png|left|200px]]
 
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==SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI GLUTAREDOXIN==
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The line below this paragraph, containing "STRUCTURE_1egr", creates the "Structure Box" on the page.
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<StructureSection load='1egr' size='340' side='right'caption='[[1egr]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[1egr]] 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=1EGR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EGR 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">Solution NMR</td></tr>
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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=1egr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1egr OCA], [https://pdbe.org/1egr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1egr RCSB], [https://www.ebi.ac.uk/pdbsum/1egr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1egr ProSAT]</span></td></tr>
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{{STRUCTURE_1egr| PDB=1egr | SCENE= }}
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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/eg/1egr_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=1egr 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 determination of the nuclear magnetic resonance structure of reduced E. coli glutaredoxin in aqueous solution is described. Based on nearly complete, sequence-specific resonance assignments, 813 nuclear Overhauser effect distance constraints and 191 dihedral angle constraints were employed 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 reduced glutaredoxin is made up of three helices and four-stranded beta-sheet. The first strand of the beta-sheet (residues 2 to 7) runs parallel to the second strand (32 to 37) and antiparallel to the third strand (61 to 64), and the sheet is extended in an antiparallel fashion with a fourth strand (67 to 69). The first helix with residues 13 to 28 and the last helix (71 to 83) run parallel to each other on one side of the beta-sheet, with their direction opposite to that of the two parallel beta-strands, and the helix formed by residues 44 to 53 fills space available due to the twist of the beta-sheet and the reduced length of the last two beta-strands. The active site Cys11-Pro-Tyr-Cys14 is located after the first beta-strand and occupies the latter part of the loop connecting this strand with the first helix.
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===SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI GLUTAREDOXIN===
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Sequence-specific 1H n.m.r. assignments and determination of the three-dimensional structure of reduced Escherichia coli glutaredoxin.,Sodano P, Xia TH, Bushweller JH, Bjornberg O, Holmgren A, Billeter M, Wuthrich K J Mol Biol. 1991 Oct 20;221(4):1311-24. PMID:1942053<ref>PMID:1942053</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_1942053}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1egr" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 1942053 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_1942053}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1EGR is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EGR OCA].
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==Reference==
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<ref group="xtra">PMID:1942053</ref><references group="xtra"/>
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Billeter, M.]]
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[[Category: Large Structures]]
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[[Category: Bjornberg, O.]]
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[[Category: Billeter M]]
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[[Category: Bushweller, J H.]]
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[[Category: Bjornberg O]]
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[[Category: Holmgren, A.]]
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[[Category: Bushweller JH]]
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[[Category: Sodano, P.]]
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[[Category: Holmgren A]]
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[[Category: Wuthrich, K.]]
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[[Category: Sodano P]]
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[[Category: Xia, T H.]]
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[[Category: Wuthrich K]]
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[[Category: Electron transport]]
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[[Category: Xia T-H]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:55:15 2009''
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Current revision

SEQUENCE-SPECIFIC 1H N.M.R. ASSIGNMENTS AND DETERMINATION OF THE THREE-DIMENSIONAL STRUCTURE OF REDUCED ESCHERICHIA COLI GLUTAREDOXIN

PDB ID 1egr

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