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4hu3
From Proteopedia
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| - | {{STRUCTURE_4hu3| PDB=4hu3 | SCENE= }} | ||
| - | ===Crystal structure of EAL domain of the E. coli DosP - monomeric form=== | ||
| - | {{ABSTRACT_PUBMED_23695249}} | ||
| - | == | + | ==Crystal structure of EAL domain of the E. coli DosP - monomeric form== |
| - | [[http://www.uniprot.org/uniprot/DOSP_ECOLI DOSP_ECOLI | + | <StructureSection load='4hu3' size='340' side='right'caption='[[4hu3]], [[Resolution|resolution]] 3.30Å' scene=''> |
| - | + | == Structural highlights == | |
| - | == | + | <table><tr><td colspan='2'>[[4hu3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HU3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HU3 FirstGlance]. <br> |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.301Å</td></tr> | |
| - | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4hu3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hu3 OCA], [https://pdbe.org/4hu3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hu3 RCSB], [https://www.ebi.ac.uk/pdbsum/4hu3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hu3 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | [[Category: | + | [https://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> |
| - | [[Category: | + | == References == |
| - | [[Category: Barends | + | <references/> |
| - | [[Category: Hartmann | + | __TOC__ |
| - | [[Category: Schlichting | + | </StructureSection> |
| - | [[Category: Tarnawski | + | [[Category: Escherichia coli K-12]] |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Barends TRM]] | |
| - | + | [[Category: Hartmann E]] | |
| - | + | [[Category: Schlichting I]] | |
| - | + | [[Category: Tarnawski M]] | |
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| - | + | ||
Current revision
Crystal structure of EAL domain of the E. coli DosP - monomeric form
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