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| ==E. coli curli protein CsgC - SeCys== | | ==E. coli curli protein CsgC - SeCys== |
- | <StructureSection load='2xsk' size='340' side='right' caption='[[2xsk]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='2xsk' size='340' side='right'caption='[[2xsk]], [[Resolution|resolution]] 1.70Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2xsk]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XSK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XSK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2xsk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XSK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XSK FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
- | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2xsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xsk OCA], [http://pdbe.org/2xsk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2xsk RCSB], [http://www.ebi.ac.uk/pdbsum/2xsk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2xsk ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2xsk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xsk OCA], [https://pdbe.org/2xsk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xsk RCSB], [https://www.ebi.ac.uk/pdbsum/2xsk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xsk ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/B2CY50_ECOLX B2CY50_ECOLX] |
| <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
- | [[Category: Cota, E]] | + | [[Category: Large Structures]] |
- | [[Category: Matthews, S J]] | + | [[Category: Cota E]] |
- | [[Category: Salgado, P S]] | + | [[Category: Matthews SJ]] |
- | [[Category: Taylor, J D]] | + | [[Category: Salgado PS]] |
- | [[Category: Chaperone]] | + | [[Category: Taylor JD]] |
| Structural highlights
Function
B2CY50_ECOLX
Publication Abstract from PubMed
The CsgC protein is a component of the curli system in Escherichia coli. Reported here is the successful incorporation of selenocysteine (SeCys) and selenomethionine (SeMet) into recombinant CsgC, yielding derivatized crystals suitable for structural determination. Unlike in previous reports, a standard autotrophic expression strain was used and only single-wavelength anomalous dispersion (SAD) data were required for successful phasing. The level of SeCys/SeMet incorporation was estimated by mass spectrometry to be about 80%. The native protein crystallized in two different crystal forms (form 1 belonging to space group C222(1) and form 2 belonging to space group C2), which diffracted to 2.4 and 2.0 A resolution, respectively, whilst Se-derivatized protein crystallized in space group C2 and diffracted to 1.7 A resolution. The Se-derivatized crystals are suitable for SAD structure determination using only the anomalous signal derived from the SeCys residues. These results extend the usability of SeCys labelling to more general and less favourable cases, rendering it a suitable alternative to traditional phasing approaches.
Extending the usability of the phasing power of diselenide bonds: SeCys SAD phasing of CsgC using a non-auxotrophic strain.,Salgado PS, Taylor JD, Cota E, Matthews SJ Acta Crystallogr D Biol Crystallogr. 2011 Jan;67(Pt 1):8-13. Epub 2010 Dec, 16. PMID:21206057[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Salgado PS, Taylor JD, Cota E, Matthews SJ. Extending the usability of the phasing power of diselenide bonds: SeCys SAD phasing of CsgC using a non-auxotrophic strain. Acta Crystallogr D Biol Crystallogr. 2011 Jan;67(Pt 1):8-13. Epub 2010 Dec, 16. PMID:21206057 doi:10.1107/S0907444910042022
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