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1gmu
From Proteopedia
(New page: 200px<br /><applet load="1gmu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gmu, resolution 1.5Å" /> '''STRUCTURE OF UREE'''<...) |
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| - | [[Image:1gmu.gif|left|200px]]<br /><applet load="1gmu" size=" | + | [[Image:1gmu.gif|left|200px]]<br /><applet load="1gmu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gmu, resolution 1.5Å" /> | caption="1gmu, resolution 1.5Å" /> | ||
'''STRUCTURE OF UREE'''<br /> | '''STRUCTURE OF UREE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | UreE is proposed to be a metallochaperone that delivers nickel ions to | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1GMU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_aerogenes Klebsiella aerogenes]. Full crystallographic information is available from [http:// | + | 1GMU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Klebsiella_aerogenes Klebsiella aerogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GMU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Hausinger, R.]] | [[Category: Hausinger, R.]] | ||
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
| - | [[Category: Mulrooney, S | + | [[Category: Mulrooney, S B.]] |
| - | [[Category: Song, H | + | [[Category: Song, H K.]] |
[[Category: metallochaperone]] | [[Category: metallochaperone]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:51:43 2008'' |
Revision as of 10:51, 21 February 2008
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STRUCTURE OF UREE
Overview
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.
About this Structure
1GMU is a Single protein structure of sequence from Klebsiella aerogenes. Full crystallographic information is available from OCA.
Reference
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
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