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PDBsum entry 1sd5

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protein metals links
Structural genomics, unknown function PDB id
1sd5
Jmol
Contents
Protein chain
188 a.a. *
Metals
IOD ×15
Waters ×206
* Residue conservation analysis
PDB id:
1sd5
Name: Structural genomics, unknown function
Title: Crystal structure of rv1626
Structure: Putative antiterminator. Chain: a. Engineered: yes. Other_details: phosphorylation dependent transcriptional antitermination regulator
Source: Mycobacterium tuberculosis. Organism_taxid: 83332. Strain: h37rv. Gene: rv1626. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
1.68Å     R-factor:   0.173     R-free:   0.216
Authors: J.P.Morth,V.Feng,L.J.Perry,D.I.Svergun,P.A.Tucker,Tb Structu Genomics Consortium (Tbsgc)
Key ref:
J.P.Morth et al. (2004). The crystal and solution structure of a putative transcriptional antiterminator from Mycobacterium tuberculosis. Structure, 12, 1595-1605. PubMed id: 15341725 DOI: 10.1016/j.str.2004.06.018
Date:
13-Feb-04     Release date:   21-Sep-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam  
P9WGM3  (PDTAR_MYCTU) -  Probable transcriptional regulatory protein pdtaR
Seq:
Struc:
205 a.a.
188 a.a.
Key:    Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cell wall   2 terms 
  Biological process     intracellular signal transduction   6 terms 
  Biochemical function     two-component response regulator activity     2 terms  

 

 
DOI no: 10.1016/j.str.2004.06.018 Structure 12:1595-1605 (2004)
PubMed id: 15341725  
 
 
The crystal and solution structure of a putative transcriptional antiterminator from Mycobacterium tuberculosis.
J.P.Morth, V.Feng, L.J.Perry, D.I.Svergun, P.A.Tucker.
 
  ABSTRACT  
 
We describe the crystal structure of Rv1626 from Mycobacterium tuberculosis at 1.48 A resolution and the corresponding solution structure determined from small angle X-ray scattering. The N-terminal domain shows structural homology to the receiver domains found in bacterial two-component systems. The C-terminal domain has high structural homology to a recently discovered RNA binding domain involved in transcriptional antitermination. The molecule in solution was found to be monomeric as it is in the crystal, but in solution it undergoes a conformational change that is triggered by changes in ionic strength. This is the first structure that links the phosphorylation cascade of the two-component systems with the antitermination event in the transcriptional machinery. Rv1626 belongs to a family of proteins, which we propose calling phosphorylation-dependent transcriptional antitermination regulators, so far only found in bacteria, and includes NasT, a protein from the assimilatory nitrate/nitrite reductase operon of Azetobacter vinelandii.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Rv1626 Superimposed with CheY and NarL(A) Superimposition of the N-terminal receiver domains of Rv1626 (red) and CheY (green).(B) Superimposition of the N-terminal receiver domains of Rv1626 (red) and NarL (cyan). Side chains believed to be involved in phosphorylation and signal propagation are shown in ball-and-stick representation. All labeling is done with respect to Rv1626. The figure was prepared in MOLSCRIPT (Kraulis, 1991) and rendered in Raster3D (Merritt and Bacon, 1997).
 
  The above figure is reprinted by permission from Cell Press: Structure (2004, 12, 1595-1605) copyright 2004.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20234377 D.A.Garsin (2010).
Ethanolamine utilization in bacterial pathogens: roles and regulation.
  Nat Rev Microbiol, 8, 290-295.  
  19436767 P.K.Rao, and Q.Li (2009).
Principal Component Analysis of Proteome Dynamics in Iron-starved Mycobacterium Tuberculosis.
  J Proteomics Bioinform, 2, 19-31.  
19506028 S.A.McMahon, G.A.Roberts, K.A.Johnson, L.P.Cooper, H.Liu, J.H.White, L.G.Carter, B.Sanghvi, M.Oke, M.D.Walkinshaw, G.W.Blakely, J.H.Naismith, and D.T.Dryden (2009).
Extensive DNA mimicry by the ArdA anti-restriction protein and its role in the spread of antibiotic resistance.
  Nucleic Acids Res, 37, 4887-4897.
PDB code: 2w82
  19052358 R.Schnell, D.Agren, and G.Schneider (2008).
1.9 A structure of the signal receiver domain of the putative response regulator NarL from Mycobacterium tuberculosis.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 1096-1100.
PDB code: 3eul
18536017 d.o. .J.Kim, J.Y.Jang, H.J.Yoon, and S.W.Suh (2008).
Crystal structure of YlqF, a circularly permuted GTPase: implications for its GTPase activation in 50 S ribosomal subunit assembly.
  Proteins, 72, 1363-1370.
PDB codes: 3cnl 3cnn 3cno
17001090 A.Geerlof, J.Brown, B.Coutard, M.P.Egloff, F.J.Enguita, M.J.Fogg, R.J.Gilbert, M.R.Groves, A.Haouz, J.E.Nettleship, P.Nordlund, R.J.Owens, M.Ruff, S.Sainsbury, D.I.Svergun, and M.Wilmanns (2006).
The impact of protein characterization in structural proteomics.
  Acta Crystallogr D Biol Crystallogr, 62, 1125-1136.  
16790934 N.Watanabe, T.Akiba, R.Kanai, and K.Harata (2006).
Structure of an orthorhombic form of xylanase II from Trichoderma reesei and analysis of thermal displacement.
  Acta Crystallogr D Biol Crystallogr, 62, 784-792.
PDB codes: 2dfb 2dfc
16154086 M.Milani, L.Leoni, G.Rampioni, E.Zennaro, P.Ascenzi, and M.Bolognesi (2005).
An active-like structure in the unphosphorylated StyR response regulator suggests a phosphorylation- dependent allosteric activation mechanism.
  Structure, 13, 1289-1297.
PDB codes: 1yio 1zn2
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.