4hu3
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hu3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hu3 RCSB], [http://www.ebi.ac.uk/pdbsum/4hu3 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hu3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hu3 RCSB], [http://www.ebi.ac.uk/pdbsum/4hu3 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/DOSP_ECOLI 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.<ref>PMID:20553324</ref> | ||
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== Publication Abstract from PubMed == | == Publication Abstract from PubMed == |
Revision as of 15:28, 25 December 2014
Crystal structure of EAL domain of the E. coli DosP - monomeric form
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