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PDBsum entry 1gmu

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protein Protein-protein interface(s) links
Metallochaperone PDB id
1gmu
Jmol
Contents
Protein chains
138 a.a. *
Waters ×962
* Residue conservation analysis
PDB id:
1gmu
Name: Metallochaperone
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
Resolution:
1.5Å     R-factor:   0.223     R-free:   0.261
Authors: H.K.Song,S.B.Mulrooney,R.Huber,R.Hausinger
Key ref: G.Obmolova et al. (1994). Crystallization and preliminary X-ray analysis of the two domains of glucosamine-6-phosphate synthase from Escherichia coli. J Mol Biol, 242, 703-705. PubMed id: 7932726
Date:
24-Sep-01     Release date:   28-Nov-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P18317  (UREE_ENTAE) -  Urease accessory protein UreE
Seq:
Struc:
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  

 

 
J Mol Biol 242:703-705 (1994)
PubMed id: 7932726  
 
 
Crystallization and preliminary X-ray analysis of the two domains of glucosamine-6-phosphate synthase from Escherichia coli.
G.Obmolova, M.A.Badet-Denisot, B.Badet, A.Teplyakov.
 
  ABSTRACT  
 
The glutamine amidohydrolase and fructose 6-phosphate binding domains of glucosamine-6-phosphate synthase from Escherichia coli have been overexpressed, purified and crystallized for X-ray diffraction analysis. The crystals of the glutamine amidohydrolase domain belong to the orthorhombic space group P2(1)2(1)2(1) with cell dimensions a = 70.4 A, b = 82.5 A, c = 86.1 A, with two molecules in the asymmetric unit, and diffract to 1.9 A resolution. The native Patterson indicated pseudo c-face centering of the unit cell. The fructose 6-phosphate binding domain was crystallized in the hexagonal space group P6(1) or P6(5) with cell dimensions a = b = 63.5 A, c = 334.3 A and with two molecules in the asymmetric unit. Diffraction data to 2.6 A resolution have been collected.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18266853 H.Barreteau, A.Kovac, A.Boniface, M.Sova, S.Gobec, and D.Blanot (2008).
Cytoplasmic steps of peptidoglycan biosynthesis.
  FEMS Microbiol Rev, 32, 168-207.  
16444800 L.T.Maillard, V.Guérineau, M.A.Badet-Denisot, B.Badet, O.Laprévote, and P.Durand (2006).
Monitoring enzyme-catalyzed production of glucosamine-6P by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry: a new enzymatic assay for glucosamine-6P synthase.
  Rapid Commun Mass Spectrom, 20, 666-672.  
11842094 K.O.Broschat, C.Gorka, J.D.Page, C.L.Martin-Berger, M.S.Davies, H.C.Huang Hc, E.A.Gulve, W.J.Salsgiver, and T.P.Kasten (2002).
Kinetic characterization of human glutamine-fructose-6-phosphate amidotransferase I: potent feedback inhibition by glucosamine 6-phosphate.
  J Biol Chem, 277, 14764-14770.  
  10091662 A.Teplyakov, G.Obmolova, M.A.Badet-Denisot, and B.Badet (1999).
The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate synthase.
  Protein Sci, 8, 596-602.
PDB code: 1mos
9933591 S.Milewski, D.Kuszczak, R.Jedrzejczak, R.J.Smith, A.J.Brown, and G.W.Gooday (1999).
Oligomeric structure and regulation of Candida albicans glucosamine-6-phosphate synthase.
  J Biol Chem, 274, 4000-4008.  
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.