1gmw

<table><tr><td colspan='2'>[[1gmw]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GMW 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></td></tr>

<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1gmu|1gmu]], [[1gmv|1gmv]]</div></td></tr>

[[https://www.uniprot.org/uniprot/UREE_ENTAE UREE_ENTAE]] Involved in urease metallocenter assembly. Binds about 6 nickel ions per homodimer. Probably functions as a nickel donor during metallocenter assembly. Its function can be bypassed in vitro in the presence of high nickel concentrations.

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== Publication Abstract from PubMed ==

UreE is proposed to be a metallochaperone that delivers nickel ions to urease during activation of this bacterial virulence factor. Wild-type Klebsiella aerogenes UreE binds approximately six nickel ions per homodimer, whereas H144*UreE (a functional C-terminal truncated variant) was previously reported to bind two. We determined the structure of H144*UreE by multi-wavelength anomalous diffraction and refined it to 1.5 A resolution. The present structure reveals an Hsp40-like peptide-binding domain, an Atx1-like metal-binding domain, and a flexible C terminus. Three metal-binding sites per dimer, defined by structural analysis of Cu-H144*UreE, are on the opposite face of the Atx1-like domain than observed in the copper metallochaperone. One metal bridges the two subunits via the pair of His-96 residues, whereas the other two sites involve metal coordination by His-110 and His-112 within each subunit. In contrast to the copper metallochaperone mechanism involving thiol ligand exchanges between structurally similar chaperones and target proteins, we propose that the Hsp40-like module interacts with urease apoprotein and/or other urease accessory proteins, while the Atx1-like domain delivers histidyl-bound nickel to the urease active site.

Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation.,Song HK, Mulrooney SB, Huber R, Hausinger RP J Biol Chem. 2001 Dec 28;276(52):49359-64. Epub 2001 Oct 8. PMID:11591723<ref>PMID:11591723</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1gmw" style="background-color:#fffaf0;"></div>

*[[Urease accessory protein|Urease accessory protein]]

[[Category: Hausinger, R]]

[[Category: Huber, R]]

[[Category: Mulrooney, S B]]

[[Category: Song, H K]]

[[Category: Metallochaperone]]