|
|
| Line 1: |
Line 1: |
| | | | |
| | ==X-ray generated oxyferrous complex of DtpA from Streptomyces lividans== | | ==X-ray generated oxyferrous complex of DtpA from Streptomyces lividans== |
| - | <StructureSection load='5map' size='340' side='right' caption='[[5map]], [[Resolution|resolution]] 1.49Å' scene=''> | + | <StructureSection load='5map' size='340' side='right'caption='[[5map]], [[Resolution|resolution]] 1.49Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5map]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_lividans_tk24 Streptomyces lividans tk24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MAP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5map]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lividans_TK24 Streptomyces lividans TK24]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MAP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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]] 1.49Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SLIV_18505 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=457428 Streptomyces lividans TK24])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=OXY:OXYGEN+MOLECULE'>OXY</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=5map FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5map OCA], [http://pdbe.org/5map PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5map RCSB], [http://www.ebi.ac.uk/pdbsum/5map PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5map 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=5map FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5map OCA], [https://pdbe.org/5map PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5map RCSB], [https://www.ebi.ac.uk/pdbsum/5map PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5map ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| Line 21: |
Line 21: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Streptomyces lividans tk24]] | + | [[Category: Large Structures]] |
| - | [[Category: Chaplin, A K]] | + | [[Category: Streptomyces lividans TK24]] |
| - | [[Category: Chicano, T Moreno]] | + | [[Category: Chaplin AK]] |
| - | [[Category: Hough, M A]] | + | [[Category: Hough MA]] |
| - | [[Category: Strange, R W]] | + | [[Category: Moreno Chicano T]] |
| - | [[Category: Worrall, J A.R]] | + | [[Category: Strange RW]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Worrall JAR]] |
| - | [[Category: Peroxidase radiolysis oxygen dye-type]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Powerful synergies are available from the combination of multiple methods to study proteins in the crystalline form. Spectroscopies which probe the same region of the crystal from which X-ray crystal structures are determined can give insights into redox, ligand and spin states to complement the information gained from the electron-density maps. The correct assignment of crystal structures to the correct protein redox and ligand states is essential to avoid the misinterpretation of structural data. This is a particular concern for haem proteins, which can occupy a wide range of redox states and are exquisitely sensitive to becoming reduced by solvated electrons generated from interactions of X-rays with water molecules in the crystal. Here, single-crystal spectroscopic fingerprinting has been applied to investigate the laser photoreduction of ferric haem in cytochrome c'. Furthermore, in situ X-ray-driven generation of haem intermediates in crystals of the dye-decolourizing-type peroxidase A (DtpA) from Streptomyces lividans is described.
Photoreduction and validation of haem-ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction.,Kekilli D, Moreno-Chicano T, Chaplin AK, Horrell S, Dworkowski FSN, Worrall JAR, Strange RW, Hough MA IUCrJ. 2017 Apr 10;4(Pt 3):263-270. doi: 10.1107/S2052252517002159. eCollection, 2017 May 1. PMID:28512573[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kekilli D, Moreno-Chicano T, Chaplin AK, Horrell S, Dworkowski FSN, Worrall JAR, Strange RW, Hough MA. Photoreduction and validation of haem-ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction. IUCrJ. 2017 Apr 10;4(Pt 3):263-270. doi: 10.1107/S2052252517002159. eCollection, 2017 May 1. PMID:28512573 doi:http://dx.doi.org/10.1107/S2052252517002159
|
