1gmw
From Proteopedia
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|PDB= 1gmw |SIZE=350|CAPTION= <scene name='initialview01'>1gmw</scene>, resolution 1.5Å | |PDB= 1gmw |SIZE=350|CAPTION= <scene name='initialview01'>1gmw</scene>, resolution 1.5Å | ||
|SITE= <scene name='pdbsite=AC1:Cu+Binding+Site+For+Chain+D'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Cu+Binding+Site+For+Chain+D'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CU:COPPER (II) ION'>CU</scene> | + | |LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gmw OCA], [http://www.ebi.ac.uk/pdbsum/1gmw PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gmw RCSB]</span> | ||
}} | }} | ||
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[[Category: Mulrooney, S B.]] | [[Category: Mulrooney, S B.]] | ||
[[Category: Song, H K.]] | [[Category: Song, H K.]] | ||
| - | [[Category: CU]] | ||
[[Category: metallochaperone]] | [[Category: metallochaperone]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:47:13 2008'' |
Revision as of 17:47, 30 March 2008
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| , resolution 1.5Å | |||||||
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| Sites: | |||||||
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
1GMW is a Protein complex structure of sequences 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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