Abstract:
:The majority of the Mycobacterium tuberculosis response to hypoxia and nitric oxide is through the DosRS (DevRS) two-component regulatory system. The N-terminal input domain of the DosS sensor contains two GAF domains. We demonstrate here that the proximal GAF domain binds haem, and identified histidine 149 of DosS as critical to haem-binding; the location of this histidine residue is similar to the cGMP-binding site in a crystal structure of cyclic nucleotide phosphodiesterase 2A. GAF domains are frequently involved in binding cyclic nucleotides, but this is the first GAF domain to be identified that binds haem. In contrast, PAS domains (similar to GAF domains in structure but not primary sequence) frequently use haem cofactors, and these findings further illustrate how the functions of these domains overlap. We propose that the activation of the DosS sensor is controlled through the haem binding of molecular oxygen or nitric oxide.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Sardiwal S,Kendall SL,Movahedzadeh F,Rison SC,Stoker NG,Djordjevic Sdoi
10.1016/j.jmb.2005.09.011keywords:
subject
Has Abstractpub_date
2005-11-11 00:00:00pages
929-36issue
5eissn
0022-2836issn
1089-8638pii
S0022-2836(05)01063-6journal_volume
353pub_type
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