7zz8: Difference between revisions
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==Cryo-EM structure of Lactococcus lactis pyruvate carboxylase with acetyl-CoA and cyclic di-AMP== | |||
<StructureSection load='7zz8' size='340' side='right'caption='[[7zz8]], [[Resolution|resolution]] 3.29Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7zz8]] 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=7ZZ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7ZZ8 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.29Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=2BA:(2R,3R,3AS,5R,7AR,9R,10R,10AS,12R,14AR)-2,9-BIS(6-AMINO-9H-PURIN-9-YL)OCTAHYDRO-2H,7H-DIFURO[3,2-D 3,2-J][1,3,7,9,2,8]TETRAOXADIPHOSPHACYCLODODECINE-3,5,10,12-TETROL+5,12-DIOXIDE'>2BA</scene>, <scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PYR:PYRUVIC+ACID'>PYR</scene></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=7zz8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zz8 OCA], [https://pdbe.org/7zz8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zz8 RCSB], [https://www.ebi.ac.uk/pdbsum/7zz8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zz8 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A2A9IR05_9LACT A0A2A9IR05_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] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Pyruvate carboxylase (PC) is a tetrameric enzyme that contains two active sites per subunit that catalyze two consecutive reactions. A mobile domain with an attached prosthetic biotin links both reactions, an initial biotin carboxylation and the subsequent carboxyl transfer to pyruvate substrate to produce oxaloacetate. Reaction sites are at long distance, and there are several co-factors that play as allosteric regulators. Here, using cryoEM we explore the structure of active PC tetramers focusing on active sites and on the conformational space of the oligomers. The results capture the mobile domain at both active sites and expose catalytic steps of both reactions at high resolution, allowing the identification of substrates and products. The analysis of catalytically active PC tetramers reveals the role of certain motions during enzyme functioning, and the structural changes in the presence of additional cofactors expose the mechanism for allosteric regulation. | |||
CryoEM structural exploration of catalytically active enzyme pyruvate carboxylase.,Lopez-Alonso JP, Lazaro M, Gil-Carton D, Choi PH, Tong L, Valle M Nat Commun. 2022 Oct 19;13(1):6185. doi: 10.1038/s41467-022-33987-2. PMID:36261450<ref>PMID:36261450</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7zz8" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
[[Category: Gil | ==See Also== | ||
[[Category: Lazaro | *[[Pyruvate carboxylase 3D structures|Pyruvate carboxylase 3D structures]] | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lactococcus lactis]] | |||
[[Category: Large Structures]] | |||
[[Category: Choi PH]] | |||
[[Category: Gil D]] | |||
[[Category: Lazaro M]] | |||
[[Category: Lopez-Alonso JP]] | |||
[[Category: Tong L]] | |||
[[Category: Valle M]] | |||
Latest revision as of 14:23, 15 November 2023
Cryo-EM structure of Lactococcus lactis pyruvate carboxylase with acetyl-CoA and cyclic di-AMPCryo-EM structure of Lactococcus lactis pyruvate carboxylase with acetyl-CoA and cyclic di-AMP
Structural highlights
FunctionA0A2A9IR05_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] Publication Abstract from PubMedPyruvate carboxylase (PC) is a tetrameric enzyme that contains two active sites per subunit that catalyze two consecutive reactions. A mobile domain with an attached prosthetic biotin links both reactions, an initial biotin carboxylation and the subsequent carboxyl transfer to pyruvate substrate to produce oxaloacetate. Reaction sites are at long distance, and there are several co-factors that play as allosteric regulators. Here, using cryoEM we explore the structure of active PC tetramers focusing on active sites and on the conformational space of the oligomers. The results capture the mobile domain at both active sites and expose catalytic steps of both reactions at high resolution, allowing the identification of substrates and products. The analysis of catalytically active PC tetramers reveals the role of certain motions during enzyme functioning, and the structural changes in the presence of additional cofactors expose the mechanism for allosteric regulation. CryoEM structural exploration of catalytically active enzyme pyruvate carboxylase.,Lopez-Alonso JP, Lazaro M, Gil-Carton D, Choi PH, Tong L, Valle M Nat Commun. 2022 Oct 19;13(1):6185. doi: 10.1038/s41467-022-33987-2. PMID:36261450[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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