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==Crystal structure of the human S-adenosylmethionine synthetase 1 in complex with the product== | ==Crystal structure of the human S-adenosylmethionine synthetase 1 in complex with the product== | ||
<StructureSection load='2obv' size='340' side='right' caption='[[2obv]], [[Resolution|resolution]] 2.05Å' scene=''> | <StructureSection load='2obv' size='340' side='right'caption='[[2obv]], [[Resolution|resolution]] 2.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2obv]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2obv]] 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=2OBV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OBV FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</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=2obv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2obv OCA], [https://pdbe.org/2obv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2obv RCSB], [https://www.ebi.ac.uk/pdbsum/2obv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2obv ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Disease == | == Disease == | ||
[ | [https://www.uniprot.org/uniprot/METK1_HUMAN METK1_HUMAN] Defects in MAT1A are the cause of methionine adenosyltransferase deficiency (MATD) [MIM:[https://omim.org/entry/250850 250850]; also called MAT I/III deficiency. MATD is an inborn error of metabolism resulting in isolated hypermethioninemia. Most patients have no clinical abnormalities, although some neurologic symptoms may be present in rare cases with severe loss of methionine adenosyltransferase activity.<ref>PMID:7560086</ref> <ref>PMID:8770875</ref> <ref>PMID:9042912</ref> <ref>PMID:10677294</ref> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/METK1_HUMAN METK1_HUMAN] Catalyzes the formation of S-adenosylmethionine from methionine and ATP. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 23: | Line 22: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2obv ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2obv ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
==See Also== | |||
*[[Methionine adenosyltransferase|Methionine adenosyltransferase]] | |||
*[[S-adenosylmethionine synthetase 3D structures|S-adenosylmethionine synthetase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Arrowsmith | [[Category: Arrowsmith CH]] | ||
[[Category: Cooper | [[Category: Cooper C]] | ||
[[Category: Edwards A]] | |||
[[Category: Edwards | [[Category: Hozjan V]] | ||
[[Category: Hozjan | [[Category: Kavanagh KL]] | ||
[[Category: Kavanagh | [[Category: Oppermann U]] | ||
[[Category: Oppermann | [[Category: Pilka ES]] | ||
[[Category: Pilka | [[Category: Shafqat N]] | ||
[[Category: Sundstrom M]] | |||
[[Category: Shafqat | [[Category: Turnbull A]] | ||
[[Category: Sundstrom | [[Category: Weigelt J]] | ||
[[Category: Turnbull | [[Category: Von Delft F]] | ||
[[Category: Weigelt | |||
[[Category: | |||
Latest revision as of 13:34, 30 August 2023
Crystal structure of the human S-adenosylmethionine synthetase 1 in complex with the productCrystal structure of the human S-adenosylmethionine synthetase 1 in complex with the product
Structural highlights
DiseaseMETK1_HUMAN Defects in MAT1A are the cause of methionine adenosyltransferase deficiency (MATD) [MIM:250850; also called MAT I/III deficiency. MATD is an inborn error of metabolism resulting in isolated hypermethioninemia. Most patients have no clinical abnormalities, although some neurologic symptoms may be present in rare cases with severe loss of methionine adenosyltransferase activity.[1] [2] [3] [4] FunctionMETK1_HUMAN Catalyzes the formation of S-adenosylmethionine from methionine and ATP. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See AlsoReferences
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