This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3u25

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:45, 14 March 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='3u25' size='340' side='right'caption='[[3u25]], [[Resolution|resolution]] 1.18&Aring;' scene=''>
<StructureSection load='3u25' size='340' side='right'caption='[[3u25]], [[Resolution|resolution]] 1.18&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[3u25]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. 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 [https://proteopedia.org/fgij/fg.htm?mol=3U25 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[3u25]] is a 2 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=3U25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3U25 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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]] 1.18&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">azu, PA4922 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</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=3u25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u25 OCA], [https://pdbe.org/3u25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u25 RCSB], [https://www.ebi.ac.uk/pdbsum/3u25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u25 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=3u25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3u25 OCA], [https://pdbe.org/3u25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3u25 RCSB], [https://www.ebi.ac.uk/pdbsum/3u25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3u25 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.
+
[https://www.uniprot.org/uniprot/AZUR_PSEAE AZUR_PSEAE] Transfers electrons from cytochrome c551 to cytochrome oxidase.
-
<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>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 3u25" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Azurin 3D structures|Azurin 3D structures]]
*[[Azurin 3D structures|Azurin 3D structures]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Gray, H B]]
+
[[Category: Pseudomonas aeruginosa]]
-
[[Category: Warren, J J]]
+
[[Category: Gray HB]]
-
[[Category: Winkler, J R]]
+
[[Category: Warren JJ]]
-
[[Category: Azurin]]
+
[[Category: Winkler JR]]
-
[[Category: Cupredoxin]]
+
-
[[Category: Electron transport]]
+

Current revision

Crystal structure of P. aeruginoas azurin containing a Tyr-His hydrogen bonded pair

PDB ID 3u25

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3u25"
Personal tools