2obv
From Proteopedia
(Difference between revisions)
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| - | + | ==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=''> | |
| - | + | == Structural highlights == | |
| - | ==Disease== | + | <table><tr><td colspan='2'>[[2obv]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2OBV FirstGlance]. <br> |
| - | [[http://www.uniprot.org/uniprot/METK1_HUMAN METK1_HUMAN]] Defects in MAT1A are the cause of methionine adenosyltransferase deficiency (MATD) [MIM:[http://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> | + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene>, <scene name='pdbligand=SAM:S-ADENOSYLMETHIONINE'>SAM</scene><br> |
| - | + | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAT1A, AMS1, MATA1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> | |
| - | ==Function== | + | <tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2obv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2obv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2obv RCSB], [http://www.ebi.ac.uk/pdbsum/2obv PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | == Disease == | ||
| + | [[http://www.uniprot.org/uniprot/METK1_HUMAN METK1_HUMAN]] Defects in MAT1A are the cause of methionine adenosyltransferase deficiency (MATD) [MIM:[http://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 == | ||
[[http://www.uniprot.org/uniprot/METK1_HUMAN METK1_HUMAN]] Catalyzes the formation of S-adenosylmethionine from methionine and ATP. | [[http://www.uniprot.org/uniprot/METK1_HUMAN METK1_HUMAN]] Catalyzes the formation of S-adenosylmethionine from methionine and ATP. | ||
| - | + | == Evolutionary Conservation == | |
| - | == | + | [[Image:Consurf_key_small.gif|200px|right]] |
| - | [[ | + | Check<jmol> |
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ob/2obv_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
| - | *[[ | + | *[[SAM synthetase|SAM synthetase]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | <references | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Methionine adenosyltransferase]] | [[Category: Methionine adenosyltransferase]] | ||
Revision as of 18:33, 30 September 2014
Crystal structure of the human S-adenosylmethionine synthetase 1 in complex with the product
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Categories: Homo sapiens | Methionine adenosyltransferase | Arrowsmith, C H. | Cooper, C. | Delft, F Von. | Edwards, A. | Hozjan, V. | Kavanagh, K L. | Oppermann, U. | Pilka, E S. | SGC, Structural Genomics Consortium. | Shafqat, N. | Sundstrom, M. | Turnbull, A. | Weigelt, J. | Sgc | Structural genomic | Structural genomics consortium | Synthetase | Transferase

