5a19: Difference between revisions
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<StructureSection load='5a19' size='340' side='right'caption='[[5a19]], [[Resolution|resolution]] 2.34Å' scene=''> | <StructureSection load='5a19' size='340' side='right'caption='[[5a19]], [[Resolution|resolution]] 2.34Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5a19]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5a19]] is a 1 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=5A19 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A19 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PPK:(DIPHOSPHONO)AMINOPHOSPHONIC+ACID'>PPK</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.34Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=PPK:(DIPHOSPHONO)AMINOPHOSPHONIC+ACID'>PPK</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=5a19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a19 OCA], [https://pdbe.org/5a19 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a19 RCSB], [https://www.ebi.ac.uk/pdbsum/5a19 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a19 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/METK2_HUMAN METK2_HUMAN] Catalyzes the formation of S-adenosylmethionine from methionine and ATP. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 5a19" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 5a19" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[S-adenosylmethionine synthetase 3D structures|S-adenosylmethionine synthetase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Antonyuk SV]] | |||
[[Category: Antonyuk | [[Category: Hasnain SS]] | ||
[[Category: Hasnain | [[Category: Lu SC]] | ||
[[Category: Lu | [[Category: Marina A]] | ||
[[Category: Marina | [[Category: Mato JM]] | ||
[[Category: Mato | [[Category: Murray B]] | ||
[[Category: Murray | [[Category: Rojas AL]] | ||
[[Category: Rojas | |||
Latest revision as of 14:02, 10 January 2024
The structure of MAT2A in complex with PPNP.The structure of MAT2A in complex with PPNP.
Structural highlights
FunctionMETK2_HUMAN Catalyzes the formation of S-adenosylmethionine from methionine and ATP. Publication Abstract from PubMedThe principal methyl donor of the cell, S-adenosylmethionine (SAMe), is produced by the highly conserved family of methionine adenosyltranferases (MATs) via an ATP-driven process. These enzymes play an important role in the preservation of life, and their dysregulation has been tightly linked to liver and colon cancers. We present crystal structures of human MATalpha2 containing various bound ligands, providing a "structural movie" of the catalytic steps. High- to atomic-resolution structures reveal the structural elements of the enzyme involved in utilization of the substrates methionine and adenosine and in formation of the product SAMe. MAT enzymes are also able to produce S-adenosylethionine (SAE) from substrate ethionine. Ethionine, an S-ethyl analog of the amino acid methionine, is known to induce steatosis and pancreatitis. We show that SAE occupies the active site in a manner similar to SAMe, confirming that ethionine also uses the same catalytic site to form the product SAE. Crystallography captures catalytic steps in human methionine adenosyltransferase enzymes.,Murray B, Antonyuk SV, Marina A, Lu SC, Mato JM, Hasnain SS, Rojas AL Proc Natl Acad Sci U S A. 2016 Feb 8. pii: 201510959. PMID:26858410[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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