5a1i: Difference between revisions

Revision as of 07:52, 18 May 2023

The structure of Human MAT2A in complex with SAM, Adenosine, Methionine and PPNP.

Structural highlights

5a1i 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.
Ligands:	ADN, EDO, K, MET, MG, PEG, PG4, PPK, SAM
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 3: / Line 3: @@
 <StructureSection load='5a1i' size='340' side='right'caption='[[5a1i]], [[Resolution|resolution]] 1.09&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5a1i]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5A1I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5A1I FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5a1i]] 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=5A1I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5A1I FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</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>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADN:ADENOSINE'>ADN</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MET:METHIONINE'>MET</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>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5a19|5a19]], [[5a1g|5a1g]]</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=5a1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1i OCA], [https://pdbe.org/5a1i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5a1i RCSB], [https://www.ebi.ac.uk/pdbsum/5a1i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5a1i ProSAT]</span></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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5a1i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5a1i OCA], [http://pdbe.org/5a1i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5a1i RCSB], [http://www.ebi.ac.uk/pdbsum/5a1i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5a1i ProSAT]</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 18: @@
 </div>
 <div class="pdbe-citations 5a1i" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[S-adenosylmethionine synthetase 3D structures|S-adenosylmethionine synthetase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Methionine adenosyltransferase]]
+[[Category: Antonyuk SV]]
-[[Category: Antonyuk, S V]]
+[[Category: Hasnain SS]]
-[[Category: Hasnain, S S]]
+[[Category: Lu SC]]
-[[Category: Lu, S C]]
+[[Category: Marina A]]
-[[Category: Marina, A]]
+[[Category: Mato JM]]
-[[Category: Mato, J M]]
+[[Category: Murray B]]
-[[Category: Murray, B]]
+[[Category: Rojas AL]]
-[[Category: Rojas, A L]]
-[[Category: Cell growth]]
-[[Category: Liver cancer]]
-[[Category: Methylation]]
-[[Category: Transferase]]

5a1i: Difference between revisions

Revision as of 07:52, 18 May 2023

The structure of Human MAT2A in complex with SAM, Adenosine, Methionine and PPNP.

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

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