1sau

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Current revision (08:30, 1 May 2024) (edit) (undo)
 
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<StructureSection load='1sau' size='340' side='right'caption='[[1sau]], [[Resolution|resolution]] 1.12&Aring;' scene=''>
<StructureSection load='1sau' size='340' side='right'caption='[[1sau]], [[Resolution|resolution]] 1.12&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1sau]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arcfu Arcfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SAU OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SAU FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1sau]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Archaeoglobus_fulgidus_DSM_4304 Archaeoglobus fulgidus DSM 4304]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SAU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SAU FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DsrC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=224325 ARCFU])</td></tr>
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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]] 1.12&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1sau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sau OCA], [http://pdbe.org/1sau PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sau RCSB], [http://www.ebi.ac.uk/pdbsum/1sau PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sau ProSAT]</span></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=1sau FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sau OCA], [https://pdbe.org/1sau PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sau RCSB], [https://www.ebi.ac.uk/pdbsum/1sau PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sau ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/O28055_ARCFU O28055_ARCFU]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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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=1sau ConSurf].
</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=1sau ConSurf].
<div style="clear:both"></div>
<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 the 115 amino-acid residue protein DsvC was determined based on the anomalous scattering provided by the five S atoms present in the structure. By collecting the diffraction data at a wavelength of 1.9 A, the anomalous signal provided by the S atoms was enhanced. However, significant radiation damage occurred during the course of the experiment, which led to differences between different parts of the data set. Only by dividing the total data set into five data sets was it possible to obtain phases; these could then be successfully extended to allow structure determination by the automated model-building program ARP/wARP. A computational correction for the radiation damage was found to significantly improve the success rate in determining the heavy-atom substructure and to improve phasing and refinement statistics.
 
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Determination of a novel structure by a combination of long-wavelength sulfur phasing and radiation-damage-induced phasing.,Weiss MS, Mander G, Hedderich R, Diederichs K, Ermler U, Warkentin E Acta Crystallogr D Biol Crystallogr. 2004 Apr;60(Pt 4):686-95. Epub 2004, Mar 23. PMID:15039557<ref>PMID:15039557</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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<div class="pdbe-citations 1sau" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Arcfu]]
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[[Category: Archaeoglobus fulgidus DSM 4304]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Ermler, U]]
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[[Category: Ermler U]]
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[[Category: Hedderich, R]]
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[[Category: Hedderich R]]
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[[Category: Kahnt, J]]
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[[Category: Kahnt J]]
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[[Category: Mander, G J]]
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[[Category: Mander GJ]]
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[[Category: Warkentin, E]]
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[[Category: Warkentin E]]
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[[Category: Weiss, M S]]
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[[Category: Weiss MS]]
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[[Category: Orthogonal helical bundle]]
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[[Category: Oxidoreductase]]
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Current revision

The Gamma subunit of the dissimilatory sulfite reductase (DsrC) from Archaeoglobus fulgidus at 1.1 A resolution

PDB ID 1sau

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