PDBsum entry 2vjw

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protein links
Hydrolase PDB id
Protein chain
138 a.a. *
Waters ×41
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Crystal structure of the second gaf domain of devs from mycobacterium smegmatis
Structure: Gaf family protein. Chain: a. Fragment: residues 232-380. Synonym: gaf-b. Engineered: yes. Other_details: 232-373 of devs protein
Source: Mycobacterium smegmatis. Organism_taxid: 1772. Expressed in: escherichia coli. Expression_system_taxid: 562.
2.00Å     R-factor:   0.210     R-free:   0.249
Authors: B.S.Kang,H.Y.Cho,H.J.Cho
Key ref: J.M.Lee et al. (2008). O2- and NO-sensing mechanism through the DevSR two-component system in Mycobacterium smegmatis. J Bacteriol, 190, 6795-6804. PubMed id: 18708494
14-Dec-07     Release date:   26-Aug-08    
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Protein chain
Pfam   ArchSchema ?
A0R2U9  (A0R2U9_MYCS2) -  GAF family protein
571 a.a.
138 a.a.
Key:    PfamA domain  Secondary structure  CATH domain


J Bacteriol 190:6795-6804 (2008)
PubMed id: 18708494  
O2- and NO-sensing mechanism through the DevSR two-component system in Mycobacterium smegmatis.
J.M.Lee, H.Y.Cho, H.J.Cho, I.J.Ko, S.W.Park, H.S.Baik, J.H.Oh, C.Y.Eom, Y.M.Kim, B.S.Kang, J.I.Oh.
The DevS histidine kinase of Mycobacterium smegmatis contains tandem GAF domains (GAF-A and GAF-B) in its N-terminal sensory domain. The heme iron of DevS is in the ferrous state when purified and is resistant to autooxidation from a ferrous to a ferric state in the presence of O(2). The redox property of the heme and the results of sequence comparison analysis indicate that DevS of M. smegmatis is more closely related to DosT of Mycobacterium tuberculosis than DevS of M. tuberculosis. The binding of O(2) to the deoxyferrous heme led to a decrease in the autokinase activity of DevS, whereas NO binding did not. The regulation of DevS autokinase activity in response to O(2) and NO was not observed in the DevS derivatives lacking its heme, indicating that the ligand-binding state of the heme plays an important role in the regulation of DevS kinase activity. The redox state of the quinone/quinol pool of the respiratory electron transport chain appears not to be implicated in the regulation of DevS activity. Neither cyclic GMP (cGMP) nor cAMP affected DevS autokinase activity, excluding the possibility that the cyclic nucleotides serve as the effector molecules to modulate DevS kinase activity. The three-dimensional structure of the putative GAF-B domain revealed that it has a GAF folding structure without cyclic nucleotide binding capacity.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20223701 J.Cheung, and W.A.Hendrickson (2010).
Sensor domains of two-component regulatory systems.
  Curr Opin Microbiol, 13, 116-123.  
20675480 M.J.Kim, K.J.Park, I.J.Ko, Y.M.Kim, and J.I.Oh (2010).
Different roles of DosS and DosT in the hypoxic adaptation of Mycobacteria.
  J Bacteriol, 192, 4868-4875.  
20523728 N.K.Taneja, S.Dhingra, A.Mittal, M.Naresh, and J.S.Tyagi (2010).
Mycobacterium tuberculosis transcriptional adaptation, growth arrest and dormancy phenotype development is triggered by vitamin C.
  PLoS One, 5, e10860.  
  20057975 B.A.Roxas, and Q.Li (2009).
Acid stress response of a mycobacterial proteome: insight from a gene ontology analysis.
  Int J Clin Exp Med, 2, 309-328.  
19276084 H.Y.Cho, H.J.Cho, Y.M.Kim, J.I.Oh, and B.S.Kang (2009).
Structural insight into the heme-based redox sensing by DosS from Mycobacterium tuberculosis.
  J Biol Chem, 284, 13057-13067.
PDB codes: 2w3d 2w3e 2w3f 2w3g 2w3h
19246238 J.Green, J.C.Crack, A.J.Thomson, and N.E.LeBrun (2009).
Bacterial sensors of oxygen.
  Curr Opin Microbiol, 12, 145-151.  
19575571 R.Gao, and A.M.Stock (2009).
Biological insights from structures of two-component proteins.
  Annu Rev Microbiol, 63, 133-154.  
19487478 R.W.Honaker, R.L.Leistikow, I.L.Bartek, and M.I.Voskuil (2009).
Unique roles of DosT and DosS in DosR regulon induction and Mycobacterium tuberculosis dormancy.
  Infect Immun, 77, 3258-3263.  
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.