4xva: Difference between revisions
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<StructureSection load='4xva' size='340' side='right' caption='[[4xva]], [[Resolution|resolution]] 2.66Å' scene=''> | <StructureSection load='4xva' size='340' side='right' caption='[[4xva]], [[Resolution|resolution]] 2.66Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xva]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XVA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XVA FirstGlance]. <br> | <table><tr><td colspan='2'>[[4xva]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XVA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XVA FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BZI:BENZIMIDAZOLE'>BZI</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BZI:BENZIMIDAZOLE'>BZI</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xv4|4xv4]], [[4xv5|4xv5]], [[4xv6|4xv6]], [[4xv7|4xv7]], [[4xv8|4xv8]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4xv4|4xv4]], [[4xv5|4xv5]], [[4xv6|4xv6]], [[4xv7|4xv7]], [[4xv8|4xv8]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CCP1, CCP, CPO, YKR066C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cytochrome-c_peroxidase Cytochrome-c peroxidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.11.1.5 1.11.1.5] </span></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=4xva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xva OCA], [http://pdbe.org/4xva PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xva RCSB], [http://www.ebi.ac.uk/pdbsum/4xva PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xva ProSAT]</span></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=4xva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xva OCA], [http://pdbe.org/4xva PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4xva RCSB], [http://www.ebi.ac.uk/pdbsum/4xva PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4xva ProSAT]</span></td></tr> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4xva" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4xva" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Baker's yeast]] | |||
[[Category: Cytochrome-c peroxidase]] | [[Category: Cytochrome-c peroxidase]] | ||
[[Category: Fischer, M]] | [[Category: Fischer, M]] | ||
Revision as of 18:36, 15 November 2017
Crystal structure of wild type cytochrome c peroxidaseCrystal structure of wild type cytochrome c peroxidase
Structural highlights
Function[CCPR_YEAST] Destroys radicals which are normally produced within the cells and which are toxic to biological systems. Publication Abstract from PubMedInterrogating fragment libraries by X-ray crystallography is a powerful strategy for discovering allosteric ligands for protein targets. Cryocooling of crystals should theoretically increase the fraction of occupied binding sites and decrease radiation damage. However, it might also perturb protein conformations that can be accessed at room temperature. Using data from crystals measured consecutively at room temperature and at cryogenic temperature, we found that transient binding sites could be abolished at the cryogenic temperatures employed by standard approaches. Changing the temperature at which the crystallographic data was collected could provide a deliberate perturbation to the equilibrium of protein conformations and help to visualize hidden sites with great potential to allosterically modulate protein function. One Crystal, Two Temperatures: Cryocooling Penalties Alter Ligand Binding to Transient Protein Sites.,Fischer M, Shoichet BK, Fraser JS Chembiochem. 2015 May 28. doi: 10.1002/cbic.201500196. PMID:26032594[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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