6q3e: Difference between revisions
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<StructureSection load='6q3e' size='340' side='right'caption='[[6q3e]], [[Resolution|resolution]] 2.03Å' scene=''> | <StructureSection load='6q3e' size='340' side='right'caption='[[6q3e]], [[Resolution|resolution]] 2.03Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6q3e]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q3E OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6q3e]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_coelicolor_A3(2) Streptomyces coelicolor A3(2)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Q3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Q3E 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></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]] 2.03Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <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></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=6q3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6q3e OCA], [https://pdbe.org/6q3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6q3e RCSB], [https://www.ebi.ac.uk/pdbsum/6q3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6q3e ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9RKQ2_STRCO Q9RKQ2_STRCO] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Appleby | [[Category: Appleby M]] | ||
[[Category: Axford | [[Category: Axford D]] | ||
[[Category: Ebrahim | [[Category: Ebrahim A]] | ||
[[Category: Moreno-Chicano | [[Category: Moreno-Chicano T]] | ||
[[Category: Owen | [[Category: Owen RL]] | ||
[[Category: Sherrell | [[Category: Sherrell DA]] | ||
[[Category: Strange | [[Category: Strange RW]] | ||
[[Category: Worrall | [[Category: Worrall JAR]] | ||
Latest revision as of 14:52, 24 January 2024
Dye type peroxidase Aa from Streptomyces lividans: 274.4 kGy structureDye type peroxidase Aa from Streptomyces lividans: 274.4 kGy structure
Structural highlights
FunctionPublication Abstract from PubMedAn approach is demonstrated to obtain, in a sample- and time-efficient manner, multiple dose-resolved crystal structures from room-temperature protein microcrystals using identical fixed-target supports at both synchrotrons and X-ray free-electron lasers (XFELs). This approach allows direct comparison of dose-resolved serial synchrotron and damage-free XFEL serial femtosecond crystallography structures of radiation-sensitive proteins. Specifically, serial synchrotron structures of a heme peroxidase enzyme reveal that X-ray induced changes occur at far lower doses than those at which diffraction quality is compromised (the Garman limit), consistent with previous studies on the reduction of heme proteins by low X-ray doses. In these structures, a functionally relevant bond length is shown to vary rapidly as a function of absorbed dose, with all room-temperature synchrotron structures exhibiting linear deformation of the active site compared with the XFEL structure. It is demonstrated that extrapolation of dose-dependent synchrotron structures to zero dose can closely approximate the damage-free XFEL structure. This approach is widely applicable to any protein where the crystal structure is altered by the synchrotron X-ray beam and provides a solution to the urgent requirement to determine intact structures of such proteins in a high-throughput and accessible manner. Dose-resolved serial synchrotron and XFEL structures of radiation-sensitive metalloproteins.,Ebrahim A, Moreno-Chicano T, Appleby MV, Chaplin AK, Beale JH, Sherrell DA, Duyvesteyn HME, Owada S, Tono K, Sugimoto H, Strange RW, Worrall JAR, Axford D, Owen RL, Hough MA IUCrJ. 2019 May 3;6(Pt 4):543-551. doi: 10.1107/S2052252519003956. eCollection, 2019 Jul 1. PMID:31316799[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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