3u25
From Proteopedia
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| - | [[ | + | ==Crystal structure of P. aeruginoas azurin containing a Tyr-His hydrogen bonded pair== |
| + | <StructureSection load='3u25' size='340' side='right' caption='[[3u25]], [[Resolution|resolution]] 1.18Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3u25]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3U25 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3U25 FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">azu, PA4922 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])</td></tr> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3u25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u25 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3u25 RCSB], [http://www.ebi.ac.uk/pdbsum/3u25 PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Redox reactions of tyrosine play key roles in many biological processes, including water oxidation and DNA synthesis. We first review the redox properties of tyrosine (and other phenols) in small molecules and related polypeptides, then report work on (H20)/(Y48)-modified Pseudomonas aeruginosa azurin. The crystal structure of this protein (1.18A resolution) shows that H20 is strongly hydrogen bonded to Y48 (2.7-2.8A tyrosine-O to histidine-N distance). A firm conclusion is that proper tuning of the tyrosine potential by a proton-accepting base is critical for biological redox functions. | ||
| - | + | Redox properties of tyrosine and related molecules.,Warren JJ, Winkler JR, Gray HB FEBS Lett. 2012 Mar 9;586(5):596-602. Epub 2011 Dec 26. PMID:22210190<ref>PMID:22210190</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Gray, H B.]] | [[Category: Gray, H B.]] | ||
Revision as of 06:44, 5 June 2014
Crystal structure of P. aeruginoas azurin containing a Tyr-His hydrogen bonded pair
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