4hu3: Difference between revisions

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{{STRUCTURE_4hu3|  PDB=4hu3  |  SCENE=  }}
===Crystal structure of EAL domain of the E. coli DosP - monomeric form===
{{ABSTRACT_PUBMED_23695249}}


==Function==
==Crystal structure of EAL domain of the E. coli DosP - monomeric form==
[[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>
<StructureSection load='4hu3' size='340' side='right'caption='[[4hu3]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<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>
[[4hu3]] is a 1 chain structure with sequence from [http://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].
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.301&#8491;</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>
==Reference==
</table>
<ref group="xtra">PMID:023695249</ref><references group="xtra"/><references/>
== Function ==
[[Category: Cyclic-guanylate-specific phosphodiesterase]]
[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: Escherichia coli k-12]]
== References ==
[[Category: Barends, T R.M.]]
<references/>
[[Category: Hartmann, E.]]
__TOC__
[[Category: Schlichting, I.]]
</StructureSection>
[[Category: Tarnawski, M.]]
[[Category: Escherichia coli K-12]]
[[Category: Cyclic di-gmp phosphodiesterase]]
[[Category: Large Structures]]
[[Category: Direct oxygen sensor]]
[[Category: Barends TRM]]
[[Category: Eal domain]]
[[Category: Hartmann E]]
[[Category: Ecdo]]
[[Category: Schlichting I]]
[[Category: Hydrolase]]
[[Category: Tarnawski M]]
[[Category: Signaling protein]]
[[Category: Tim-barrel]]

Latest revision as of 11:44, 1 March 2024

Crystal structure of EAL domain of the E. coli DosP - monomeric form

4hu3, resolution 3.30Å

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