PDBsum entry 1gmw

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protein metals Protein-protein interface(s) links
Chaperone PDB id
Protein chains
138 a.a. *
_CU ×6
Waters ×164
* Residue conservation analysis
PDB id:
Name: Chaperone
Title: Structure of uree
Structure: Uree. Chain: a, b, c, d. Fragment: residues 1-143. Engineered: yes. Mutation: yes
Source: Klebsiella aerogenes. Organism_taxid: 28451. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Monomer (from PDB file)
1.5Å     R-factor:   0.223     R-free:   0.261
Authors: H.K.Song,S.B.Mulrooney,R.Huber,R.Hausinger
Key ref:
H.K.Song et al. (2001). Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation. J Biol Chem, 276, 49359-49364. PubMed id: 11591723 DOI: 10.1074/jbc.M108619200
24-Sep-01     Release date:   28-Nov-01    
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Protein chains
Pfam   ArchSchema ?
P18317  (UREE_ENTAE) -  Urease accessory protein UreE
158 a.a.
138 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     protein complex assembly   4 terms 
  Biochemical function     metal ion binding     2 terms  


DOI no: 10.1074/jbc.M108619200 J Biol Chem 276:49359-49364 (2001)
PubMed id: 11591723  
Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation.
H.K.Song, S.B.Mulrooney, R.Huber, R.P.Hausinger.
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.
  Selected figure(s)  
Figure 2.
Fig. 2. Structural homology of UreE domains to Atx1 and Sis1. Ribbon diagrams are shown comparing the overall structures of the metal-binding domain of UreE (a), Atx1 copper chaperone (b), putative peptide-binding domain of UreE (c), and domain I of Sis1 (d). Metal-binding residues and bound metal ions are indicated (His-96, His-110, His-112, and Cu2+ in UreE; Cys-15, Cys-18, and Hg2+ in Atx1). Residues 1-13 and 130-138 in the UreE structure are not included for clarity.
Figure 3.
Fig. 3. Surface representations of H144*UreE. a and c, residues forming the hydrophobic surfaces of UreE are colored green and labeled. Bound-copper ions are shown as red balls. b and d, residues that have previously been subjected to mutagenesis are colored magenta and labeled in one subunit, and those in the other are colored blue and labeled with a prime ('). Bound-copper ions are shown as green balls. The view in a and b is the same as that in Fig. 1a, and the view in c and d is obtained by a 180° rotation around a vertical axis. Figs. were drawn with GRASP (47).
  The above figures are reprinted by permission from the ASBMB: J Biol Chem (2001, 276, 49359-49364) copyright 2001.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20207756 E.L.Carter, and R.P.Hausinger (2010).
Characterization of the Klebsiella aerogenes urease accessory protein UreD in fusion with the maltose binding protein.
  J Bacteriol, 192, 2294-2304.  
20442959 H.Kaluarachchi, K.C.Chan Chung, and D.B.Zamble (2010).
Microbial nickel proteins.
  Nat Prod Rep, 27, 681-694.  
20333422 O.E.Johnson, K.C.Ryan, M.J.Maroney, and T.C.Brunold (2010).
Spectroscopic and computational investigation of three Cys-to-Ser mutants of nickel superoxide dismutase: insight into the roles played by the Cys2 and Cys6 active-site residues.
  J Biol Inorg Chem, 15, 777-793.  
20635345 R.Lam, V.Romanov, K.Johns, K.P.Battaile, J.Wu-Brown, J.L.Guthrie, R.P.Hausinger, E.F.Pai, and N.Y.Chirgadze (2010).
Crystal structure of a truncated urease accessory protein UreF from Helicobacter pylori.
  Proteins, 78, 2839-2848.
PDB code: 3cxn
19822009 C.E.Haas, D.A.Rodionov, J.Kropat, D.Malasarn, S.S.Merchant, and Crécy-Lagard (2009).
A subset of the diverse COG0523 family of putative metal chaperones is linked to zinc homeostasis in all kingdoms of life.
  BMC Genomics, 10, 470.  
  20046957 E.L.Carter, N.Flugga, J.L.Boer, S.B.Mulrooney, and R.P.Hausinger (2009).
Interplay of metal ions and urease.
  Metallomics, 1, 207-221.  
19476442 M.Bellucci, B.Zambelli, F.Musiani, P.Turano, and S.Ciurli (2009).
Helicobacter pylori UreE, a urease accessory protein: specific Ni(2+)- and Zn(2+)-binding properties and interaction with its cognate UreG.
  Biochem J, 422, 91.  
18823937 S.Quiroz-Valenzuela, S.C.Sukuru, R.P.Hausinger, L.A.Kuhn, and W.T.Heller (2008).
The structure of urease activation complexes examined by flexibility analysis, mutagenesis, and small-angle X-ray scattering.
  Arch Biochem Biophys, 480, 51-57.  
17242515 C.Addy, M.Ohara, F.Kawai, A.Kidera, M.Ikeguchi, S.Fuchigami, M.Osawa, I.Shimada, S.Y.Park, J.R.Tame, and J.G.Heddle (2007).
Nickel binding to NikA: an additional binding site reconciles spectroscopy, calorimetry and crystallography.
  Acta Crystallogr D Biol Crystallogr, 63, 221-229.
PDB code: 2noo
17637984 D.P.Giedroc, and A.I.Arunkumar (2007).
Metal sensor proteins: nature's metalloregulated allosteric switches.
  Dalton Trans, (), 3107-3120.  
17205208 R.J.Maier, S.L.Benoit, and S.Seshadri (2007).
Nickel-binding and accessory proteins facilitating Ni-enzyme maturation in Helicobacter pylori.
  Biometals, 20, 655-664.  
17041056 J.K.Kim, S.B.Mulrooney, and R.P.Hausinger (2006).
The UreEF fusion protein provides a soluble and functional form of the UreF urease accessory protein.
  J Bacteriol, 188, 8413-8420.  
15950874 M.Yamanishi, M.Vlasie, and R.Banerjee (2005).
Adenosyltransferase: an enzyme and an escort for coenzyme B12?
  Trends Biochem Sci, 30, 304-308.  
15866948 S.B.Mulrooney, S.K.Ward, and R.P.Hausinger (2005).
Purification and properties of the Klebsiella aerogenes UreE metal-binding domain, a functional metallochaperone of urease.
  J Bacteriol, 187, 3581-3585.  
12655048 I.Bertini, and A.Rosato (2003).
Bioinorganic chemistry in the postgenomic era.
  Proc Natl Acad Sci U S A, 100, 3601-3604.  
12486048 S.B.Mulrooney, and R.P.Hausinger (2003).
Metal ion dependence of recombinant Escherichia coli allantoinase.
  J Bacteriol, 185, 126-134.  
12829270 S.B.Mulrooney, and R.P.Hausinger (2003).
Nickel uptake and utilization by microorganisms.
  FEMS Microbiol Rev, 27, 239-261.  
12896998 S.Benoit, and R.J.Maier (2003).
Dependence of Helicobacter pylori urease activity on the nickel-sequestering ability of the UreE accessory protein.
  J Bacteriol, 185, 4787-4795.  
12655069 S.C.Burdette, and S.J.Lippard (2003).
Meeting of the minds: metalloneurochemistry.
  Proc Natl Acad Sci U S A, 100, 3605-3610.  
12079778 A.C.Rosenzweig (2002).
Metallochaperones: bind and deliver.
  Chem Biol, 9, 673-677.  
  12426116 P.E.Carrington, F.Al-Mjeni, M.A.Zoroddu, M.Costa, and M.J.Maroney (2002).
Use of XAS for the elucidation of metal structure and function: applications to nickel biochemistry, molecular toxicology, and carcinogenesis.
  Environ Health Perspect, 110, 705-708.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.