5o25
From Proteopedia
(Difference between revisions)
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<StructureSection load='5o25' size='340' side='right' caption='[[5o25]], [[Resolution|resolution]] 1.75Å' scene=''> | <StructureSection load='5o25' size='340' side='right' caption='[[5o25]], [[Resolution|resolution]] 1.75Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5o25]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O25 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O25 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5o25]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43589 Atcc 43589]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O25 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5O25 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5o1u|5o1u]], [[5o4z|5o4z]], [[5o58|5o58]], [[5o70|5o70]], [[5o7f|5o7f]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5o1u|5o1u]], [[5o4z|5o4z]], [[5o58|5o58]], [[5o70|5o70]], [[5o7f|5o7f]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_1595 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2336 ATCC 43589])</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=5o25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o25 OCA], [http://pdbe.org/5o25 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o25 RCSB], [http://www.ebi.ac.uk/pdbsum/5o25 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o25 ProSAT]</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=5o25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o25 OCA], [http://pdbe.org/5o25 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5o25 RCSB], [http://www.ebi.ac.uk/pdbsum/5o25 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5o25 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The concentration of messenger molecules in bacterial cells needs to be tightly regulated. This can be achieved by either controlling the synthesis rate, degradation, or export by specific transporters, respectively. The regulation of the essential second messenger c-di-AMP is achieved by modulation of the diadenylate cyclase activity as well as by specific phosphodiesterases that hydrolyze c-di-AMP in the cell. We provide here structural and biochemical data on the DHH-type phosphodiesterase TmPDE (TM1595) from Thermotoga maritima. Our analysis shows that TmPDE is preferentially degrading linear dinucleotides, such as 5'-pApA, 5'-pGpG, and 5'-pApG, compared with cyclic dinucleotide substrates. The high-resolution structural data provided here describe all steps of the PDE reaction: the ligand-free enzyme, two substrate-bound states, and three post-reaction states. We can furthermore show that Pde2 from Streptococcus pneumoniae shares both structural features and substrate specificity based on small-angle X-ray scattering data and biochemical assays. | ||
| + | |||
| + | Structural and Biophysical Analysis of the Soluble DHH/DHHA1-Type Phosphodiesterase TM1595 from Thermotoga maritima.,Drexler DJ, Muller M, Rojas-Cordova CA, Bandera AM, Witte G Structure. 2017 Oct 24. pii: S0969-2126(17)30329-5. doi:, 10.1016/j.str.2017.10.001. PMID:29107484<ref>PMID:29107484</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5o25" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Atcc 43589]] | ||
[[Category: Drexler, D]] | [[Category: Drexler, D]] | ||
[[Category: Mueller, M]] | [[Category: Mueller, M]] | ||
Revision as of 10:12, 15 November 2017
Structure of wildtype T.maritima PDE (TM1595) in ligand-free state
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