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PDBsum entry 4xxh
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protein ligands Protein-protein interface(s) links
Gene regulation PDB id
4xxh

 

 

 

 

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Contents
Protein chains
255 a.a.
Ligands
GLC-G6P ×2
Waters ×79
PDB id:
4xxh
Name: Gene regulation
Title: Trehalose repressor from escherichia coli
Structure: Hth-type transcriptional regulator trer. Chain: a, b. Fragment: effector binding domain, unp residues 61-315. Synonym: trehalose operon repressor
Source: Escherichia coli k-12. Organism_taxid: 83333
Resolution:
2.40Å     R-factor:   0.152     R-free:   0.173
Authors: U.Hars,R.Horlacher,W.Boos,O.S.Smart,G.Bricogne,W.Welte,K.Diederichs
Key ref:
U.Hars et al. (1998). Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose. Protein Sci, 7, 2511-2521. PubMed id: 9865945 DOI: 10.1002/pro.5560071204
Date:
30-Jan-15     Release date:   11-Feb-15    
Supersedes: 1byk
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P36673  (TRER_ECOLI) -  HTH-type transcriptional regulator TreR from Escherichia coli (strain K12)
Seq:
Struc: 		315 a.a.
255 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

 

 
DOI no: 10.1002/pro.5560071204 Protein Sci 7:2511-2521 (1998)
PubMed id: 9865945  
 
 
Crystal structure of the effector-binding domain of the trehalose-repressor of Escherichia coli, a member of the LacI family, in its complexes with inducer trehalose-6-phosphate and noninducer trehalose.
U.Hars, R.Horlacher, W.Boos, W.Welte, K.Diederichs.
 
  ABSTRACT  
 
The crystal structure of the Escherichia coli trehalose repressor (TreR) in a complex with its inducer trehalose-6-phosphate was determined by the method of multiple isomorphous replacement (MIR) at 2.5 A resolution, followed by the structure determination of TreR in a complex with its noninducer trehalose at 3.1 A resolution. The model consists of residues 61 to 315 comprising the effector binding domain, which forms a dimer as in other members of the LacI family. This domain is composed of two similar subdomains each consisting of a central beta-sheet sandwiched between alpha-helices. The effector binding pocket is at the interface of these subdomains. In spite of different physiological functions, the crystal structures of the two complexes of TreR turned out to be virtually identical to each other with the conformation being similar to those of the effector binding domains of the LacI and PurR in complex with their effector molecules. According to the crystal structure, the noninducer trehalose binds to a similar site as the trehalose portion of trehalose-6-phosphate. The binding affinity for the former is lower than for the latter. The noninducer trehalose thus binds competitively to the repressor. Unlike the phosphorylated inducer molecule, it is incapable of blocking the binding of the repressor headpiece to its operator DNA. The ratio of the concentrations of trehalose-6-phosphate and trehalose thus is used to switch between the two alternative metabolic uses of trehalose as an osmoprotectant and as a carbon source.
 
  Selected figure(s)  
 
Figure 1.
Fig. 1. Structure of theTreR effector bindindmaindimerwithboundinducermoleculeTre6P in ribbonrepresentation.Th/-strands are colore blue ndnamedAthrough K. The a-helices are inyellowandnamedsequentiallyas I through X. Thegraphicwasmade with MOLSCRIPT(Kraulis,1991).TheN-terminalsubdoainiscomposed of strandA(64-69),heix I (75-91). trand B (94-99), helix II (104-115), strand C(121-124),heli III 132-138). strandD(142-144),strandE(153-157).helix X (284-299).andstrand K (307-310). The C-terminalsubdomain consists of helix IV (159-172),strand F (178-181),helix (192-204).strandG(210-212), helix VI (218-224),helix VII (226-228), strand H (235-238),helix VIII (241-253), strand 260-264).helix M (268-273),and strand J (278-281).Theconnectingcross-over are at residues 157-158,282-283,and310-311. 		Figure 3.
Fig. 3. Scheme of hydrogenbonds of Tre6PinitscomplexwithTreR.Thedistancesbetweenacceptors an donorsaregiven A.
 
  The above figures are reprinted from an Open Access publication published by the Protein Society: Protein Sci (1998, 7, 2511-2521) copyright 1998.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21374721 S.Tungtur, D.J.Parente, and L.Swint-Kruse (2011).
Functionally important positions can comprise the majority of a protein's architecture.
  Proteins, 79, 1589-1608.  
18470695 S.J.Lee, M.Surma, W.Hausner, M.Thomm, and W.Boos (2008).
The role of TrmB and TrmB-like transcriptional regulators for sugar transport and metabolism in the hyperthermophilic archaeon Pyrococcus furiosus.
  Arch Microbiol, 190, 247-256.  
17372346 B.Loll, M.Kowalczyk, C.Alings, A.Chieduch, J.Bardowski, W.Saenger, and J.Biesiadka (2007).
Structure of the transcription regulator CcpA from Lactococcus lactis.
  Acta Crystallogr D Biol Crystallogr, 63, 431-436.
PDB code: 2o20
17636568 Q.S.Xu, I.Ankoudinova, Y.Lou, H.Yokota, R.Kim, and S.H.Kim (2007).
Crystal structure of a transcriptional activator of comK gene from Bacillus halodurans.
  Proteins, 69, 409-414.
PDB code: 2hqb
16585763 I.S.Franco, L.J.Mota, C.M.Soares, and I.de Sá-Nogueira (2006).
Functional domains of the Bacillus subtilis transcription factor AraR and identification of amino acids important for nucleoprotein complex assembly and effector binding.
  J Bacteriol, 188, 3024-3036.  
16815921 K.N.Rao, D.Kumaran, J.Seetharaman, J.B.Bonanno, S.K.Burley, and S.Swaminathan (2006).
Crystal structure of trehalose-6-phosphate phosphatase-related protein: biochemical and biological implications.
  Protein Sci, 15, 1735-1744.
PDB code: 1u02
11266612 L.Swint-Kruse, C.R.Elam, J.W.Lin, D.R.Wycuff, and K.Shive Matthews (2001).
Plasticity of quaternary structure: twenty-two ways to form a LacI dimer.
  Protein Sci, 10, 262-276.  
10737762 J.M.Johnson, and G.M.Church (2000).
Predicting ligand-binding function in families of bacterial receptors.
  Proc Natl Acad Sci U S A, 97, 3965-3970.  
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.

 

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