8e8o: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[8e8o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8E8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8E8O FirstGlance]. <br>
<table><tr><td colspan='2'>[[8e8o]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8E8O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8E8O FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.77&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=8e8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8e8o OCA], [https://pdbe.org/8e8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8e8o RCSB], [https://www.ebi.ac.uk/pdbsum/8e8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8e8o 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=8e8o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8e8o OCA], [https://pdbe.org/8e8o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8e8o RCSB], [https://www.ebi.ac.uk/pdbsum/8e8o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8e8o ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/MAON_HUMAN MAON_HUMAN] Catalyzes the oxidative decarboxylation of (S)-malate to pyruvate using NADP(+) as a cofactor (PubMed:7818469). Can also reverse the decarboxylation reaction, but only with significantly lower efficiency (PubMed:7818469).<ref>PMID:7818469</ref>  
[https://www.uniprot.org/uniprot/MAON_HUMAN MAON_HUMAN] Catalyzes the oxidative decarboxylation of (S)-malate to pyruvate using NADP(+) as a cofactor (PubMed:7818469). Can also reverse the decarboxylation reaction, but only with significantly lower efficiency (PubMed:7818469).<ref>PMID:7818469</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Malic enzymes (ME1, ME2, and ME3) are involved in cellular energy regulation, redox homeostasis, and biosynthetic processes, through the production of pyruvate and reducing agent NAD(P)H. Recent studies have implicated the third and least well-characterized isoform, mitochondrial NADP(+)-dependent malic enzyme 3 (ME3), as a therapeutic target for pancreatic cancers. Here, we utilized an integrated structure approach to determine the structures of ME3 in various ligand-binding states at near-atomic resolutions. ME3 is captured in the open form existing as a stable tetramer and its dynamic Domain C is critical for activity. Catalytic assay results reveal that ME3 is a non-allosteric enzyme and does not require modulators for activity while structural analysis suggests that the inner stability of ME3 Domain A relative to ME2 disables allostery in ME3. With structural information available for all three malic enzymes, the foundation has been laid to understand the structural and biochemical differences of these enzymes and could aid in the development of specific malic enzyme small molecule drugs.


Integrative structural and functional analysis of human malic enzyme 3: A potential therapeutic target for pancreatic cancer.,Grell TAJ, Mason M, Thompson AA, Gomez-Tamayo JC, Riley D, Wagner MV, Steele R, Ortiz-Meoz RF, Wadia J, Shaffer PL, Tresadern G, Sharma S, Yu X Heliyon. 2022 Dec 19;8(12):e12392. doi: 10.1016/j.heliyon.2022.e12392. , eCollection 2022 Dec. PMID:36590518<ref>PMID:36590518</ref>
==See Also==
 
*[[NADP-dependent malic enzyme|NADP-dependent malic enzyme]]
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8e8o" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>

Latest revision as of 09:33, 19 June 2024

Cryo-EM structure of human ME3 in the presence of citrateCryo-EM structure of human ME3 in the presence of citrate

Structural highlights

8e8o is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 2.77Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

MAON_HUMAN Catalyzes the oxidative decarboxylation of (S)-malate to pyruvate using NADP(+) as a cofactor (PubMed:7818469). Can also reverse the decarboxylation reaction, but only with significantly lower efficiency (PubMed:7818469).[1]

See Also

References

  1. ↑ Loeber G, Maurer-Fogy I, Schwendenwein R. Purification, cDNA cloning and heterologous expression of the human mitochondrial NADP(+)-dependent malic enzyme. Biochem J. 1994 Dec 15;304 ( Pt 3)(Pt 3):687-92. PMID:7818469 doi:10.1042/bj3040687

8e8o, resolution 2.77Å

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