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PDBsum entry 1e2b

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protein links
Transferase PDB id
1e2b
Jmol
Contents
Protein chain
106 a.a. *
* Residue conservation analysis
PDB id:
1e2b
Name: Transferase
Title: Nmr structure of the c10s mutant of enzyme iib cellobiose of phosphoenol-pyruvate dependent phosphotransferase system of escherichia coli, 17 structures
Structure: Enzyme iib-cellobiose. Chain: a. Engineered: yes. Mutation: yes
Source: Escherichia coli. Organism_taxid: 83333. Strain: k12. Cellular_location: cytoplasm. Gene: cela. Expressed in: escherichia coli str. K12 substr. W3110. Expression_system_taxid: 316407.
NMR struc: 17 models
Authors: E.Ab,G.Schuurman-Wolters,J.Reizer,M.H.Saier,K.Dijkstra,R.M.S G.T.Robillard
Key ref: E.Ab et al. (1997). The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli. Protein Sci, 6, 304-314. PubMed id: 9041631 DOI: 10.1002/pro.5560060205
Date:
15-Nov-96     Release date:   23-Jul-97    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P69795  (PTQB_ECOLI) -  N,N'-diacetylchitobiose-specific phosphotransferase enzyme IIB component
Seq:
Struc:
106 a.a.
106 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.2.7.1.69  - Protein-N(pi)-phosphohistidine--sugar phosphotransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein EIIB N(pi)-phospho-L-histidine/cysteine + sugar = protein EIIB + sugar phosphate

+
=
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Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   2 terms 
  Biological process     transport   6 terms 
  Biochemical function     transferase activity     4 terms  

 

 
    Key reference    
 
 
DOI no: 10.1002/pro.5560060205 Protein Sci 6:304-314 (1997)
PubMed id: 9041631  
 
 
The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.
E.Ab, G.Schuurman-Wolters, J.Reizer, M.H.Saier, K.Dijkstra, R.M.Scheek, G.T.Robillard.
 
  ABSTRACT  
 
The assignment of the side-chain NMR resonances and the determination of the three-dimensional solution structure of the C10S mutant of enzyme IIBcellobiose (IIBcel) of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli are presented. The side-chain resonances were assigned nearly completely using a variety of mostly heteronuclear NMR experiments, including HCCH-TOCSY, HCCH-COSY, and COCCH-TOCSY experiments as well as CBCACOHA, CBCA(CO)NH, and HBHA(CBCA)(CO)NH experiments. In order to obtain the three-dimensional structure, NOE data were collected from 15N-NOESY-HSQC, 13C-HSQC-NOESY, and 2D NOE experiments. The distance restraints derived from these NOE data were used in distance geometry calculations followed by molecular dynamics and simulated annealing protocols. In an iterative procedure, additional NOE assignments were derived from the calculated structures and new structures were calculated. The final set of structures, calculated with approximately 2000 unambiguous and ambiguous distance restraints, has an rms deviation of 1.1 A on C alpha atoms. IIBcel consists of a four stranded parallel beta-sheet, in the order 2134. The sheet is flanked with two and three alpha-helices on either side. Residue 10, a cysteine in the wild-type enzyme, which is phosphorylated during the catalytic cycle, is located at the end of the first beta-strand. A loop that is proposed to be involved in the binding of the phosphoryl-group follows the cysteine. The loop appears to be disordered in the unphosphorylated state.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19959833 Y.S.Jung, M.Cai, and G.M.Clore (2010).
Solution structure of the IIAChitobiose-IIBChitobiose complex of the N,N'-diacetylchitobiose branch of the Escherichia coli phosphotransferase system.
  J Biol Chem, 285, 4173-4184.
PDB codes: 2wwv 2wy2
17158705 J.Deutscher, C.Francke, and P.W.Postma (2006).
How phosphotransferase system-related protein phosphorylation regulates carbohydrate metabolism in bacteria.
  Microbiol Mol Biol Rev, 70, 939.  
16963640 L.Volpon, C.R.Young, A.Matte, and K.Gehring (2006).
NMR structure of the enzyme GatB of the galactitol-specific phosphoenolpyruvate-dependent phosphotransferase system and its interaction with GatA.
  Protein Sci, 15, 2435-2441.
PDB code: 1tvm
16195543 C.L.Gustafson, C.V.Stauffacher, K.Hallenga, and R.L.Van Etten (2005).
Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop.
  Protein Sci, 14, 2515-2525.
PDB code: 1p8a
11573087 I.Zegers, J.C.Martins, R.Willem, L.Wyns, and J.Messens (2001).
Arsenate reductase from S. aureus plasmid pI258 is a phosphatase drafted for redox duty.
  Nat Struct Biol, 8, 843-847.
PDB codes: 1jf8 1jfv
11060015 G.Wang, J.M.Louis, M.Sondej, Y.J.Seok, A.Peterkofsky, and G.M.Clore (2000).
Solution structure of the phosphoryl transfer complex between the signal transducing proteins HPr and IIA(glucose) of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system.
  EMBO J, 19, 5635-5649.
PDB code: 1ggr
  10210178 T.Kernebeck, S.Pflanz, G.Müller-Newen, G.Kurapkat, R.M.Scheek, K.Dijkstra, P.C.Heinrich, A.Wollmer, S.Grzesiek, and J.Grötzinger (1999).
The signal transducer gp130: solution structure of the carboxy-terminal domain of the cytokine receptor homology region.
  Protein Sci, 8, 5.
PDB code: 1bj8
9261069 P.Sliz, R.Engelmann, W.Hengstenberg, and E.F.Pai (1997).
The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system.
  Structure, 5, 775-788.
PDB code: 1e2a
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 codes are shown on the right.

 

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