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5mjh
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray generated oxyferrous/water mixed complex of DtpA from Streptomyces lividans== | |
| + | <StructureSection load='5mjh' size='340' side='right'caption='[[5mjh]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5mjh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_lividans_1326 Streptomyces lividans 1326]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MJH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MJH FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.45Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=5mjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mjh OCA], [https://pdbe.org/5mjh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mjh RCSB], [https://www.ebi.ac.uk/pdbsum/5mjh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mjh ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:28512573</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5mjh" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: Strange | + | </StructureSection> |
| + | [[Category: Large Structures]] | ||
| + | [[Category: Streptomyces lividans 1326]] | ||
| + | [[Category: Chaplin AK]] | ||
| + | [[Category: Hough MA]] | ||
| + | [[Category: Moreno Chicano T]] | ||
| + | [[Category: Strange RW]] | ||
| + | [[Category: Worrall JAR]] | ||
Current revision
X-ray generated oxyferrous/water mixed complex of DtpA from Streptomyces lividans
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