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| | ==Crystal Structure of L. monocytogenes phosphodiesterase PgpH HD domain== | | ==Crystal Structure of L. monocytogenes phosphodiesterase PgpH HD domain== |
| - | <StructureSection load='4s1c' size='340' side='right' caption='[[4s1c]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='4s1c' size='340' side='right'caption='[[4s1c]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4s1c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lismo Lismo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S1C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4S1C FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4s1c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_EGD-e Listeria monocytogenes EGD-e]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4S1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4S1C FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4s1b|4s1b]]</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=4s1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s1c OCA], [https://pdbe.org/4s1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4s1c RCSB], [https://www.ebi.ac.uk/pdbsum/4s1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4s1c ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lmo1466, pgpH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=169963 LISMO])</td></tr>
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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=4s1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4s1c OCA], [http://pdbe.org/4s1c PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4s1c RCSB], [http://www.ebi.ac.uk/pdbsum/4s1c PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4s1c ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q8Y746_LISMO Q8Y746_LISMO] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Lismo]] | + | [[Category: Large Structures]] |
| - | [[Category: Luo, S]] | + | [[Category: Listeria monocytogenes EGD-e]] |
| - | [[Category: Tong, L]]
| + | [[Category: Luo S]] |
| - | [[Category: C-di-amp]]
| + | [[Category: Tong L]] |
| - | [[Category: Hd domain]] | + | |
| - | [[Category: Hydrolase]] | + | |
| - | [[Category: Listeria monocytogene]]
| + | |
| - | [[Category: Phosphodiesterase]]
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| Structural highlights
Function
Q8Y746_LISMO
Publication Abstract from PubMed
The nucleotide cyclic di-3',5'- adenosine monophosphate (c-di-AMP) was recently identified as an essential and widespread second messenger in bacterial signaling. Among c-di-AMP-producing bacteria, altered nucleotide levels result in several physiological defects and attenuated virulence. Thus, a detailed molecular understanding of c-di-AMP metabolism is of both fundamental and practical interest. Currently, c-di-AMP degradation is recognized solely among DHH-DHHA1 domain-containing phosphodiesterases. Using chemical proteomics, we identified the Listeria monocytogenes protein PgpH as a molecular target of c-di-AMP. Biochemical and structural studies revealed that the PgpH His-Asp (HD) domain bound c-di-AMP with high affinity and specifically hydrolyzed this nucleotide to 5'-pApA. PgpH hydrolysis activity was inhibited by ppGpp, indicating a cross-talk between c-di-AMP signaling and the stringent response. Genetic analyses supported coordinated regulation of c-di-AMP levels in and out of the host. Intriguingly, a L. monocytogenes mutant that lacks c-di-AMP phosphodiesterases exhibited elevated c-di-AMP levels, hyperinduced a host type-I IFN response, and was significantly attenuated for infection. Furthermore, PgpH homologs, which belong to the 7TMR-HD family, are widespread among hundreds of c-di-AMP synthesizing microorganisms. Thus, PgpH represents a broadly conserved class of c-di-AMP phosphodiesterase with possibly other physiological functions in this crucial signaling network.
An HD-domain phosphodiesterase mediates cooperative hydrolysis of c-di-AMP to affect bacterial growth and virulence.,Huynh TN, Luo S, Pensinger D, Sauer JD, Tong L, Woodward JJ Proc Natl Acad Sci U S A. 2015 Jan 12. pii: 201416485. PMID:25583510[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Huynh TN, Luo S, Pensinger D, Sauer JD, Tong L, Woodward JJ. An HD-domain phosphodiesterase mediates cooperative hydrolysis of c-di-AMP to affect bacterial growth and virulence. Proc Natl Acad Sci U S A. 2015 Jan 12. pii: 201416485. PMID:25583510 doi:http://dx.doi.org/10.1073/pnas.1416485112
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