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PDBsum entry 1e2a
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protein metals Protein-protein interface(s) links
Transferase PDB id
1e2a

 

 

 

 

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Contents
Protein chains
102 a.a. *
Metals
_MG
Waters ×56
* Residue conservation analysis
PDB id:
1e2a
Name: Transferase
Title: Enzyme iia from the lactose specific pts from lactococcus lactis
Structure: Enzyme iia. Chain: a, b, c. Synonym: enzyme iii, lactose-specific iia component. Engineered: yes
Source: Lactococcus lactis. Organism_taxid: 1358. Strain: mg1820. Gene: lacf. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Homo-Trimer (from PDB file)
Resolution:
2.30Å     R-factor:   0.190     R-free:   0.240
Authors: P.Sliz,R.Engelmann,W.Hengstenberg,E.F.Pai
Key ref:
P.Sliz et al. (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. PubMed id: 9261069 DOI: 10.1016/S0969-2126(97)00232-3
Date:
25-Apr-97     Release date:   29-Apr-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P23532  (PTLA_LACLL) -  PTS system lactose-specific EIIA component from Lactococcus lactis subsp. lactis
Seq:
Struc: 		105 a.a.
102 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.1.69  - Transferred entry: 2.7.1.191, 2.7.1.192, 2.7.1.193, 2.7.1.194, 2.7.1.195,
[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

 

 
    Key reference    
 
 
DOI no: 10.1016/S0969-2126(97)00232-3 Structure 5:775-788 (1997)
PubMed id: 9261069  
 
 
The structure of enzyme IIAlactose from Lactococcus lactis reveals a new fold and points to possible interactions of a multicomponent system.
P.Sliz, R.Engelmann, W.Hengstenberg, E.F.Pai.
 
  ABSTRACT  
 
BACKGROUND: The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is responsible for the binding, transmembrane transport and phosphorylation of numerous sugar substrates. The system is also involved in the regulation of a variety of metabolic and transcriptional processes. The PTS consists of two non-specific energy coupling components, enzyme I and a heat stable phosphocarrier protein (HPr), as well as several sugar-specific multiprotein permeases known as enzymes II. In most cases, enzymes IIA and IIB are located in the cytoplasm, while enzyme IIC acts as a membrane channel. Enzyme IIAlactose belongs to the lactose/cellobiose-specific family of enzymes II, one of four functionally and structurally distinct groups. The protein, which normally functions as a trimer, is believed to separate into its subunits after phosphorylation. RESULTS: The crystal structure of the trimeric enzyme IIAlactose from Lactococcus lactis has been determined at 2.3 A resolution. The subunits of the enzyme, related to each other by the inherent threefold rotational symmetry, possess interesting structural features such as coiled-coil-like packing and a methionine cluster. The subunits each comprise three helices (I, II and III) and pack against each other forming a nine-helix bundle. This helical bundle is stabilized by a centrally located metal ion and also encloses a hydrophobic cavity. The three phosphorylation sites (His78 on each monomer) are located in helices III and their sidechains protrude into a large groove between helices I and II of the neighbouring subunits. A model of the complex between phosphorylated HPr and enzyme IIAlactose has been constructed. CONCLUSIONS: Enzyme IIAlactose is the first representative of the family of lactose/cellobiose-specific enzymes IIA for which a three-dimensional structure has been determined. Some of its structural features, like the presence of two histidine residues at the active site, seem to be common to all enzymes no overall structural homology is observed to any PTS proteins or to any other proteins in the Protein Data Bank. Enzyme IIAlactose shows surface complementarity to the phosphorylated form of HPr and several energetically favourable interactions between the two molecules can be predicted.
 
  Selected figure(s)  
 
Figure 8.
Figure 8. Stereo view representation of a modelled enzyme IIA-HPr complex. With knowledge of the phosphorylation site, the family of NMR structures of P-HPr (PDB code 1PFH coloured in red) was docked into the crystallographic model of enzyme IIA. The P-HPr ensemble of structures was rotated around the apical axis (red line) to minimize clashes and short contacts between the two proteins. Residues possibly involved in electrostatic interaction are Glu64[IIA] and Arg17[HPr]. Sidechains of His78[IIA], His82[IIA] and P-His15[HPr] are displayed and coloured by atom type.
 
  The above figure is reprinted by permission from Cell Press: Structure (1997, 5, 775-788) copyright 1997.  
  Figure was selected by the author.  

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.  
16443929 J.Y.Suh, M.Cai, D.C.Williams, and G.M.Clore (2006).
Solution structure of a post-transition state analog of the phosphotransfer reaction between the A and B cytoplasmic domains of the mannitol transporter IIMannitol of the Escherichia coli phosphotransferase system.
  J Biol Chem, 281, 8939-8949.
PDB code: 2few
15654077 C.Tang, D.C.Williams, R.Ghirlando, and G.M.Clore (2005).
Solution structure of enzyme IIA(Chitobiose) from the N,N'-diacetylchitobiose branch of the Escherichia coli phosphotransferase system.
  J Biol Chem, 280, 11770-11780.
PDB code: 1wcr
15258141 P.M.Legler, M.Cai, A.Peterkofsky, and G.M.Clore (2004).
Three-dimensional solution structure of the cytoplasmic B domain of the mannitol transporter IImannitol of the Escherichia coli phosphotransferase system.
  J Biol Chem, 279, 39115-39121.
PDB code: 1vkr
15347589 W.R.Silverman, J.P.Bannister, and D.M.Papazian (2004).
Binding site in eag voltage sensor accommodates a variety of ions and is accessible in closed channel.
  Biophys J, 87, 3110-3121.  
12202490 G.Cornilescu, B.R.Lee, C.C.Cornilescu, G.Wang, A.Peterkofsky, and G.M.Clore (2002).
Solution structure of the phosphoryl transfer complex between the cytoplasmic A domain of the mannitol transporter IIMannitol and HPr of the Escherichia coli phosphotransferase system.
  J Biol Chem, 277, 42289-42298.
PDB code: 1j6t
12169623 M.Witty, C.Sanz, A.Shah, J.G.Grossmann, K.Mizuguchi, R.N.Perham, and B.Luisi (2002).
Structure of the periplasmic domain of Pseudomonas aeruginosa TolA: evidence for an evolutionary relationship with the TonB transporter protein.
  EMBO J, 21, 4207-4218.
PDB code: 1lr0
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
  11055995 W.R.Silverman, C.Y.Tang, A.F.Mock, K.B.Huh, and D.M.Papazian (2000).
Mg(2+) modulates voltage-dependent activation in ether-à-go-go potassium channels by binding between transmembrane segments S2 and S3.
  J Gen Physiol, 116, 663-678.  
10425677 A.Mattevi, G.Tedeschi, L.Bacchella, A.Coda, A.Negri, and S.Ronchi (1999).
Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family.
  Structure, 7, 745-756.
PDB code: 1chu
10393270 G.T.Robillard, and J.Broos (1999).
Structure/function studies on the bacterial carbohydrate transporters, enzymes II, of the phosphoenolpyruvate-dependent phosphotransferase system.
  Biochim Biophys Acta, 1422, 73.  
10037691 R.Gutknecht, K.Flükiger, R.Lanz, and B.Erni (1999).
Mechanism of phosphoryl transfer in the dimeric IIABMan subunit of the Escherichia coli mannose transporter.
  J Biol Chem, 274, 6091-6096.  
9565750 J.P.Schneider, A.Lombardi, and W.F.DeGrado (1998).
Analysis and design of three-stranded coiled coils and three-helix bundles.
  Fold Des, 3, R29-R40.  
  9655345 J.W.Bryson, J.R.Desjarlais, T.M.Handel, and W.F.DeGrado (1998).
From coiled coils to small globular proteins: design of a native-like three-helix bundle.
  Protein Sci, 7, 1404-1414.  
9551558 R.L.van Montfort, T.Pijning, K.H.Kalk, I.Hangyi, M.L.Kouwijzer, G.T.Robillard, and B.W.Dijkstra (1998).
The structure of the Escherichia coli phosphotransferase IIAmannitol reveals a novel fold with two conformations of the active site.
  Structure, 6, 377-388.
PDB code: 1a3a
9434897 M.M.McEvoy, and F.W.Dahlquist (1997).
Phosphohistidines in bacterial signaling.
  Curr Opin Struct Biol, 7, 793-797.  
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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