1r1c: Difference between revisions
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<StructureSection load='1r1c' size='340' side='right'caption='[[1r1c]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1r1c' size='340' side='right'caption='[[1r1c]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1r1c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1r1c]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R1C FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=REP:(1,10+PHENANTHROLINE)-(TRI-CARBON+MONOXIDE)+RHENIUM+(I)'>REP</scene> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene>, <scene name='pdbligand=REP:(1,10+PHENANTHROLINE)-(TRI-CARBON+MONOXIDE)+RHENIUM+(I)'>REP</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=1r1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1c OCA], [https://pdbe.org/1r1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r1c RCSB], [https://www.ebi.ac.uk/pdbsum/1r1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r1c 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=1r1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r1c OCA], [https://pdbe.org/1r1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r1c RCSB], [https://www.ebi.ac.uk/pdbsum/1r1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r1c ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Crane | [[Category: Crane BR]] | ||
[[Category: | [[Category: Di Bilio AJ]] | ||
[[Category: | [[Category: Gradinaru C]] | ||
[[Category: | [[Category: Miller JE]] | ||
Revision as of 08:59, 23 August 2023
PSEUDOMONAS AERUGINOSA W48F/Y72F/H83Q/Y108W-AZURIN RE(PHEN)(CO)3(HIS107)PSEUDOMONAS AERUGINOSA W48F/Y72F/H83Q/Y108W-AZURIN RE(PHEN)(CO)3(HIS107)
Structural highlights
FunctionAZUR_PSEAE Transfers electrons from cytochrome c551 to cytochrome oxidase. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNear-UV irradiation of structurally characterized [Re(I)(CO)3(1,10-phenanthroline)(Q107H)](W48F/Y72F/H83Q/Y108W)AzM(II) [Az = Pseudomonas aeruginosa azurin, M = Cu, Zn]/[Co(NH3)5Cl]Cl2 produces a tryptophan radical (W108*) with unprecedented kinetic stability. After rapid formation (k = 2.8 x 106 s-1), the radical persists for more than 5 h at room temperature in the folded ReAzM(II) structure. The absorption spectrum of ReAz(W108*)M(II) exhibits maxima at 512 and 536 nm. Oxidation of K4[Mo(CN)8] by ReAz(W108*)Zn(II) places the W108*/W108 reduction potential in the protein above 0.8 V vs NHE. Spectroscopy and reactivity of a photogenerated tryptophan radical in a structurally defined protein environment.,Miller JE, Gradinaru C, Crane BR, Di Bilio AJ, Wehbi WA, Un S, Winkler JR, Gray HB J Am Chem Soc. 2003 Nov 26;125(47):14220-1. PMID:14624538[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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