5a19: Difference between revisions

Latest revision as of 11:02, 10 January 2024

The structure of MAT2A in complex with PPNP.

Structural highlights

5a19 is a 1 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:	X-ray diffraction, Resolution 2.34Å
Ligands:	EDO, K, MG, PEG, PG4, PPK
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

METK2_HUMAN Catalyzes the formation of S-adenosylmethionine from methionine and ATP.

Publication Abstract from PubMed

The 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.

References

↑ Murray B, Antonyuk SV, Marina A, Lu SC, Mato JM, Hasnain SS, Rojas AL. Crystallography captures catalytic steps in human methionine adenosyltransferase enzymes. Proc Natl Acad Sci U S A. 2016 Feb 8. pii: 201510959. PMID:26858410 doi:https://dx.doi.org/10.1073/pnas.1510959113

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OCA

[1] Murray B, Antonyuk SV, Marina A, Lu SC, Mato JM, Hasnain SS, Rojas AL. Crystallography captures catalytic steps in human methionine adenosyltransferase enzymes. Proc Natl Acad Sci U S A. 2016 Feb 8. pii: 201510959. PMID:26858410 doi:https://dx.doi.org/10.1073/pnas.1510959113

[1]

@@ Line 1: / Line 1: @@
 ==The structure of MAT2A in complex with PPNP.==
-<StructureSection load='5a19' size='340' side='right' caption='[[5a19]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
+<StructureSection load='5a19' size='340' side='right'caption='[[5a19]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5a19]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A19 FirstGlance]. <br>
+<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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.34&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a1g|5a1g]], [[5a1i|5a1i]]</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.6 2.5.1.6] </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=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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a19 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a19 OCA], [http://pdbe.org/5a19 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a19 RCSB], [http://www.ebi.ac.uk/pdbsum/5a19 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/METK2_HUMAN METK2_HUMAN]] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
+[https://www.uniprot.org/uniprot/METK2_HUMAN METK2_HUMAN] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 19: @@
 </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/>
 __TOC__
 </StructureSection>
-[[Category: Methionine adenosyltransferase]]
+[[Category: Homo sapiens]]
-[[Category: Antonyuk, S V]]
+[[Category: Large Structures]]
-[[Category: Hasnain, S S]]
+[[Category: Antonyuk SV]]
-[[Category: Lu, S C]]
+[[Category: Hasnain SS]]
-[[Category: Marina, A]]
+[[Category: Lu SC]]
-[[Category: Mato, J M]]
+[[Category: Marina A]]
-[[Category: Murray, B]]
+[[Category: Mato JM]]
-[[Category: Rojas, A L]]
+[[Category: Murray B]]
-[[Category: Cell growth]]
+[[Category: Rojas AL]]
-[[Category: Liver cancer]]
-[[Category: Methylation]]
-[[Category: Transferase]]

5a19: Difference between revisions

Latest revision as of 11:02, 10 January 2024

The structure of MAT2A in complex with PPNP.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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