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PDBsum entry 2vbz

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protein ligands Protein-protein interface(s) links
DNA binding protein PDB id
2vbz

 

 

 

 

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Contents
Protein chains
147 a.a. *
Ligands
TRP
Waters ×43
* Residue conservation analysis
PDB id:
2vbz
Name: DNA binding protein
Title: Feast or famine regulatory protein (rv3291c)from m. Tuberculosis complexed with l-tryptophan
Structure: Transcriptional regulatory protein. Chain: a, b. Synonym: rv3291c, leucine-responsive regulatory protein, asnc-family. Engineered: yes
Source: Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
2.80Å     R-factor:   0.207     R-free:   0.253
Authors: T.Shrivastava,R.Ramachandran
Key ref: T.Shrivastava and R.Ramachandran (2007). Mechanistic insights from the crystal structures of a feast/famine regulatory protein from Mycobacterium tuberculosis H37Rv. Nucleic Acids Res, 35, 7324-7335. PubMed id: 17962306
Date:
18-Sep-07     Release date:   06-Nov-07    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P96896  (P96896_MYCTO) -  Leucine-responsive regulatory protein from Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Seq:
Struc:
150 a.a.
147 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
Nucleic Acids Res 35:7324-7335 (2007)
PubMed id: 17962306  
 
 
Mechanistic insights from the crystal structures of a feast/famine regulatory protein from Mycobacterium tuberculosis H37Rv.
T.Shrivastava, R.Ramachandran.
 
  ABSTRACT  
 
Rv3291c gene from Mycobacterium tuberculosis codes for a transcriptional regulator belonging to the (leucine responsive regulatory protein/regulator of asparigine synthase C gene product) Lrp/AsnC-family. We have identified a novel effector-binding site from crystal structures of the apo protein, complexes with a variety of amino acid effectors, X-ray based ligand screening and qualitative fluorescence spectroscopy experiments. The new effector site is in addition to the structural characterization of another distinct site in the protein conserved in the related AsnC-family of regulators. The structures reveal that the ligand-binding loops of two crystallographically independent subunits adopt different conformations to generate two distinct effector-binding sites. A change in the conformation of the binding site loop 100-106 in the B subunit is apparently necessary for octameric association and also allows the loop to interact with a bound ligand in the newly identified effector-binding site. There are four sites of each kind in the octamer and the protein preferentially binds to aromatic amino acids. While amino acids like Phe, Tyr and Trp exhibit binding to only one site, His exhibits binding to both sites. Binding of Phe is accompanied by a conformational change of 3.7 A in the 75-83 loop, which is advantageously positioned to control formation of higher oligomers. Taken together, the present studies suggest an elegant control mechanism for global transcription regulation involving binding of ligands to the two sites, individually or collectively.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19170871 E.Peeters, S.V.Albers, A.Vassart, A.J.Driessen, and D.Charlier (2009).
Ss-LrpB, a transcriptional regulator from Sulfolobus solfataricus, regulates a gene cluster with a pyruvate ferredoxin oxidoreductase-encoding operon and permease genes.
  Mol Microbiol, 71, 972-988.  
19004003 M.Yamada, S.A.Ishijima, and M.Suzuki (2009).
Interactions between the archaeal transcription repressor FL11 and its coregulators lysine and arginine.
  Proteins, 74, 520-525.
PDB codes: 2zny 2znz
18653535 T.Kumarevel, N.Nakano, K.Ponnuraj, S.C.Gopinath, K.Sakamoto, A.Shinkai, P.K.Kumar, and S.Yokoyama (2008).
Crystal structure of glutamine receptor protein from Sulfolobus tokodaii strain 7 in complex with its effector L-glutamine: implications of effector binding in molecular association and DNA binding.
  Nucleic Acids Res, 36, 4808-4820.
PDB codes: 2e7w 2e7x 2efn 2efo 2efp 2efq 2pmh 2pn6 2yx4 2yx7
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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