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==Crystal structure of the EAL domain of c-di-GMP specific phosphodiesterase YahA in complex with activating cofactor Mg++== | ==Crystal structure of the EAL domain of c-di-GMP specific phosphodiesterase YahA in complex with activating cofactor Mg++== | ||
<StructureSection load='4lyk' size='340' side='right' caption='[[4lyk]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='4lyk' size='340' side='right' caption='[[4lyk]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kie|4kie]], [[4lj3|4lj3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4kie|4kie]], [[4lj3|4lj3]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0315, JW0307, yahA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">b0315, JW0307, yahA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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=4lyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lyk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lyk RCSB], [http://www.ebi.ac.uk/pdbsum/4lyk 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=4lyk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lyk OCA], [http://pdbe.org/4lyk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lyk RCSB], [http://www.ebi.ac.uk/pdbsum/4lyk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lyk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4lyk" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 21:15, 4 August 2016
Crystal structure of the EAL domain of c-di-GMP specific phosphodiesterase YahA in complex with activating cofactor Mg++Crystal structure of the EAL domain of c-di-GMP specific phosphodiesterase YahA in complex with activating cofactor Mg++
Structural highlights
Function[YAHA_ECOLI] Hydrolyzes c-di-GMP (cyclic bis(3'-5') dimeric GMP) to 5'-pGpG, known as PDE-A activity. PDE-B activity, that is hydrolysis of 5'-pGpG to GMP, proceeds only very slowly. Publication Abstract from PubMedThe universal second messenger cyclic di-GMP (cdG) is involved in the regulation of a diverse range of cellular processes in bacteria. The intracellular concentration of the dinucleotide is determined by the opposing actions of diguanylate cyclases (DGCs) and cdG specific phosphodiesterases (PDEs). While most PDEs have accessory domains that are involved in the regulation of their activity, the regulatory mechanism of this class of enzymes has remained unclear. Here, we use biophysical and functional analyses to show that the isolated EAL domain of a PDE from E. coli (YahA) is in a fast thermodynamic monomer - dimer equilibrium, and that the domain is active only in its dimeric state. Furthermore, our data indicate thermodynamic coupling between substrate binding and EAL dimerization with the dimerization affinity being increased about 100-fold upon substrate binding. Crystal structures of the YahA-EAL domain determined under various conditions (apo, Mg2+, c-di-GMP/Mg2+ complex) confirm structural coupling between the dimer interface and the catalytic center. The in-built regulatory properties of the EAL domain probably facilitates its modular, functional combination with the diverse repertoire of accessory domains. Inherent regulation of EAL domain-catalyzed hydrolysis of second messenger c-di-GMP.,Sundriyal A, Massa C, Samoray D, Zehender F, Sharpe T, Jenal U, Schirmer T J Biol Chem. 2014 Jan 22. PMID:24451384[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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