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| ==Crystal structure of Lactococcus lactis pyruvate carboxylase== | | ==Crystal structure of Lactococcus lactis pyruvate carboxylase== |
| <StructureSection load='5vyw' size='340' side='right' caption='[[5vyw]], [[Resolution|resolution]] 3.10Å' scene=''> | | <StructureSection load='5vyw' size='340' side='right'caption='[[5vyw]], [[Resolution|resolution]] 3.10Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[5vyw]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VYW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5VYW FirstGlance]. <br> | | <table><tr><td colspan='2'>[[5vyw]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5VYW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5VYW FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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]] 3.1Å</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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></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=5vyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vyw OCA], [http://pdbe.org/5vyw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5vyw RCSB], [http://www.ebi.ac.uk/pdbsum/5vyw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5vyw ProSAT]</span></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=5vyw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5vyw OCA], [https://pdbe.org/5vyw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5vyw RCSB], [https://www.ebi.ac.uk/pdbsum/5vyw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5vyw ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function ==
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| [[http://www.uniprot.org/uniprot/A0A089XIW4_9LACT A0A089XIW4_9LACT]] 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]
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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Cyclic di-3',5'-adenosine monophosphate (c-di-AMP) is a broadly conserved bacterial second messenger that has been implicated in a wide range of cellular processes. Our earlier studies showed that c-di-AMP regulates central metabolism in Listeria monocytogenes by inhibiting its pyruvate carboxylase (LmPC), a biotin-dependent enzyme with biotin carboxylase (BC) and carboxyltransferase (CT) activities. We report here structural, biochemical, and functional studies on the inhibition of Lactococcus lactis PC (LlPC) by c-di-AMP. The compound is bound at the dimer interface of the CT domain, at a site equivalent to that in LmPC, although it has a distinct binding mode in the LlPC complex. This binding site is not well conserved among PCs, and only a subset of these bacterial enzymes are sensitive to c-di-AMP. Conformational changes in the CT dimer induced by c-di-AMP binding may be the molecular mechanism for its inhibitory activity. Mutations of residues in the binding site can abolish c-di-AMP inhibition. In L. lactis, LlPC is required for efficient milk acidification through its essential role in aspartate biosynthesis. The aspartate pool in L. lactis is negatively regulated by c-di-AMP, and high aspartate levels can be restored by expression of a c-di-AMP-insensitive LlPC. LlPC has high intrinsic catalytic activity and is not sensitive to acetyl-CoA activation, in contrast to other PC enzymes.
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| Structural and functional studies of pyruvate carboxylase regulation by cyclic di-AMP in lactic acid bacteria.,Choi PH, Vu TMN, Pham HT, Woodward JJ, Turner MS, Tong L Proc Natl Acad Sci U S A. 2017 Aug 14. pii: 201704756. doi:, 10.1073/pnas.1704756114. PMID:28808024<ref>PMID:28808024</ref>
| | ==See Also== |
| | | *[[Pyruvate carboxylase 3D structures|Pyruvate carboxylase 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 5vyw" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Pyruvate carboxylase]] | | [[Category: Lactococcus lactis]] |
| [[Category: Choi, P H]] | | [[Category: Large Structures]] |
| [[Category: Tong, L]] | | [[Category: Choi PH]] |
| [[Category: Biotin-dependent carboxylase tim-barrel cyclic-di-amp]] | | [[Category: Tong L]] |
| [[Category: Ligase]]
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