View source for 2vow


==An oxidized tryptophan facilitates copper-binding in Methylococcus capsulatus secreted protein MopE. The structure of recombinant MopE to 1.65AA==
<StructureSection load='2vow' size='340' side='right'caption='[[2vow]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2vow]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Methylococcus_capsulatus_str._Bath Methylococcus capsulatus str. Bath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VOW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=2vow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vow OCA], [https://pdbe.org/2vow PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vow RCSB], [https://www.ebi.ac.uk/pdbsum/2vow PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vow ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/G1UBC6_METCA G1UBC6_METCA] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Proteins can coordinate metal ions with endogenous nitrogen and oxygen ligands through backbone amino and carbonyl groups, but the amino acid side chains coordinating metals do not include tryptophan. Here we show for the first time the involvement of the tryptophan metabolite kynurenine in a protein metal-binding site. The crystal structure to 1.35A of MopE(*) from the methane-oxidizing Methylococcus capsulatus (Bath) provided detailed information about its structure and mononuclear copper-binding site. MopE(*) contains a novel protein fold of which only one-third of the structure displays similarities to other known folds. The geometry around the copper ion is distorted tetrahedral with one oxygen ligand from a water molecule, two histidine imidazoles (His-132 and His-203), and at the fourth distorted tetrahedral position, the N1 atom of the kynurenine, an oxidation product of Trp-130. Trp-130 was not oxidized to kynurenine in MopE(*) heterologously expressed in Escherichia coli, nor did this protein bind copper. Our findings indicate that the modification of tryptophan to kynurenine and its involvement in copper binding is an innate property of M. capsulatus MopE(*).

An Oxidized Tryptophan Facilitates Copper Binding in Methylococcus capsulatus-secreted Protein MopE.,Helland R, Fjellbirkeland A, Karlsen OA, Ve T, Lillehaug JR, Jensen HB J Biol Chem. 2008 May 16;283(20):13897-904. Epub 2008 Mar 18. PMID:18348978<ref>PMID:18348978</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2vow" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Methylococcus capsulatus str. Bath]]
[[Category: Fjellbirkeland A]]
[[Category: Helland R]]
[[Category: Jensen HB]]
[[Category: Karlsen OA]]
[[Category: Lillehaug JR]]
[[Category: Ve T]]