4hu4 | pdb_00004hu4
Crystal structure of EAL domain of the E. coli DosP - dimeric form
Template:ABSTRACT PUBMED 23695249
Function
[DOSP_ECOLI] Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP (PubMed:15995192) but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate (PubMed:11970957). Via its PDE activity on c-di-GMP, DosP regulates biofilm formation through the repression of transcription of the csgBAC operon, which encodes curli structural subunits.[1]
About this Structure
4hu4 is a 2 chain structure with sequence from Escherichia coli k-12. Full crystallographic information is available from OCA.
Reference
- Tarnawski M, Barends TR, Hartmann E, Schlichting I. Structures of the catalytic EAL domain of the Escherichia coli direct oxygen sensor. Acta Crystallogr D Biol Crystallogr. 2013 Jun;69(Pt 6):1045-53. doi:, 10.1107/S0907444913004423. Epub 2013 May 14. PMID:23695249 doi:10.1107/S0907444913004423
- ↑ Tagliabue L, Maciag A, Antoniani D, Landini P. The yddV-dos operon controls biofilm formation through the regulation of genes encoding curli fibers' subunits in aerobically growing Escherichia coli. FEMS Immunol Med Microbiol. 2010 Aug;59(3):477-84. doi:, 10.1111/j.1574-695X.2010.00702.x. Epub 2010 May 20. PMID:20553324 doi:10.1111/j.1574-695X.2010.00702.x
