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| | <StructureSection load='4qsl' size='340' side='right'caption='[[4qsl]], [[Resolution|resolution]] 3.28Å' scene=''> | | <StructureSection load='4qsl' size='340' side='right'caption='[[4qsl]], [[Resolution|resolution]] 3.28Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4qsl]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_monocytogenes_hominis"_nyfeldt_1932 "bacterium monocytogenes hominis" nyfeldt 1932]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QSL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4QSL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4qsl]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes Listeria monocytogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4QSL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4QSL FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4qsh|4qsh]], [[4qsk|4qsk]]</td></tr> | + | </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=4qsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qsl OCA], [https://pdbe.org/4qsl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4qsl RCSB], [https://www.ebi.ac.uk/pdbsum/4qsl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4qsl ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AX24_02755 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1639 "Bacterium monocytogenes hominis" Nyfeldt 1932])</td></tr>
| + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyruvate_carboxylase Pyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.4.1.1 6.4.1.1] </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=4qsl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qsl OCA], [http://pdbe.org/4qsl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4qsl RCSB], [http://www.ebi.ac.uk/pdbsum/4qsl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4qsl ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| - | == Function == | |
| - | [[http://www.uniprot.org/uniprot/W6G6F5_LISMN W6G6F5_LISMN]] Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.[PIRNR:PIRNR001594] | |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 4qsl" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 4qsl" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Pyruvate carboxylase 3D structures|Pyruvate carboxylase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium monocytogenes hominis nyfeldt 1932]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Pyruvate carboxylase]] | + | [[Category: Listeria monocytogenes]] |
| - | [[Category: Choi, P H]] | + | [[Category: Choi PH]] |
| - | [[Category: Tong, L]] | + | [[Category: Tong L]] |
| - | [[Category: Acetyl-coa]]
| + | |
| - | [[Category: Biotin]]
| + | |
| - | [[Category: Ligase]]
| + | |
| - | [[Category: Tim barrell]]
| + | |
| Structural highlights
Publication Abstract from PubMed
Cyclic di-adenosine monophosphate (c-di-AMP) is a broadly conserved second messenger required for bacterial growth and infection. However, the molecular mechanisms of c-di-AMP signaling are still poorly understood. Using a chemical proteomics screen for c-di-AMP-interacting proteins in the pathogen Listeria monocytogenes, we identified several broadly conserved protein receptors, including the central metabolic enzyme pyruvate carboxylase (LmPC). Biochemical and crystallographic studies of the LmPC-c-di-AMP interaction revealed a previously unrecognized allosteric regulatory site 25 A from the active site. Mutations in this site disrupted c-di-AMP binding and affected catalytic activity of LmPC as well as PC from pathogenic Enterococcus faecalis. C-di-AMP depletion resulted in altered metabolic activity in L. monocytogenes. Correction of this metabolic imbalance rescued bacterial growth, reduced bacterial lysis, and resulted in enhanced bacterial burdens during infection. These findings greatly expand the c-di-AMP signaling repertoire and reveal a central metabolic regulatory role for a cyclic dinucleotide.
The cyclic dinucleotide c-di-AMP is an allosteric regulator of metabolic enzyme function.,Sureka K, Choi PH, Precit M, Delince M, Pensinger DA, Huynh TN, Jurado AR, Goo YA, Sadilek M, Iavarone AT, Sauer JD, Tong L, Woodward JJ Cell. 2014 Sep 11;158(6):1389-401. doi: 10.1016/j.cell.2014.07.046. PMID:25215494[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sureka K, Choi PH, Precit M, Delince M, Pensinger DA, Huynh TN, Jurado AR, Goo YA, Sadilek M, Iavarone AT, Sauer JD, Tong L, Woodward JJ. The cyclic dinucleotide c-di-AMP is an allosteric regulator of metabolic enzyme function. Cell. 2014 Sep 11;158(6):1389-401. doi: 10.1016/j.cell.2014.07.046. PMID:25215494 doi:http://dx.doi.org/10.1016/j.cell.2014.07.046
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