7pk5
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7pk5]] is a 4 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=7PK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PK5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7pk5]] is a 4 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=7PK5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PK5 FirstGlance]. <br> | ||
| - | </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=7pk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pk5 OCA], [https://pdbe.org/7pk5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pk5 RCSB], [https://www.ebi.ac.uk/pdbsum/7pk5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pk5 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.4Å</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=7pk5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pk5 OCA], [https://pdbe.org/7pk5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pk5 RCSB], [https://www.ebi.ac.uk/pdbsum/7pk5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pk5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/PDEL_ECOLI PDEL_ECOLI] Acts both as an enzyme and as a c-di-GMP sensor to couple transcriptional activity to the c-di-GMP status of the cell (PubMed:26553851). Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic-di-GMP (c-di-GMP) to 5'-pGpG (PubMed:15995192, PubMed:24451384, PubMed:26553851). Also acts as a transcription factor to control its own expression (PubMed:26553851).<ref>PMID:15995192</ref> <ref>PMID:24451384</ref> <ref>PMID:26553851</ref> | |
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Phosphodiesterase PdeL (EAL domain of crystals comprising full-length protein)
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