2obv: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
← Older editNewer edit →
No edit summary
No edit summary
Line 1: Line 1:


==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]] 2.05&Aring;' scene=''>
<StructureSection load='2obv' size='340' side='right'caption='[[2obv]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2obv]] 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=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>
<table><tr><td colspan='2'>[[2obv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. 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='ligand'><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></td></tr>
</td></tr><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='gene'><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 HUMAN])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MAT1A, AMS1, MATA1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Methionine_adenosyltransferase Methionine adenosyltransferase], with EC number [https://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=2obv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2obv OCA], [http://pdbe.org/2obv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2obv RCSB], [http://www.ebi.ac.uk/pdbsum/2obv PDBsum], [http://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'>[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>
</table>
</table>
== Disease ==
== 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>   
[[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 ==
[[http://www.uniprot.org/uniprot/METK1_HUMAN METK1_HUMAN]] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.  
[[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 23:
</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==
*[[SAM synthetase|SAM synthetase]]
== References ==
== References ==
<references/>
<references/>
Line 28: Line 31:
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Methionine adenosyltransferase]]
[[Category: Methionine adenosyltransferase]]
[[Category: Arrowsmith, C H]]
[[Category: Arrowsmith, C H]]

Revision as of 15:52, 9 June 2021

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

2obv is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Gene:MAT1A, AMS1, MATA1 (HUMAN)
Activity:Methionine adenosyltransferase, with EC number 2.5.1.6
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[METK1_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]

Function

[METK1_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 Also

References

  1. ↑ Ubagai T, Lei KJ, Huang S, Mudd SH, Levy HL, Chou JY. Molecular mechanisms of an inborn error of methionine pathway. Methionine adenosyltransferase deficiency. J Clin Invest. 1995 Oct;96(4):1943-7. PMID:7560086 doi:http://dx.doi.org/10.1172/JCI118240
  2. ↑ Chamberlin ME, Ubagai T, Mudd SH, Wilson WG, Leonard JV, Chou JY. Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency. J Clin Invest. 1996 Aug 15;98(4):1021-7. PMID:8770875 doi:10.1172/JCI118862
  3. ↑ Chamberlin ME, Ubagai T, Mudd SH, Levy HL, Chou JY. Dominant inheritance of isolated hypermethioninemia is associated with a mutation in the human methionine adenosyltransferase 1A gene. Am J Hum Genet. 1997 Mar;60(3):540-6. PMID:9042912
  4. ↑ Chamberlin ME, Ubagai T, Mudd SH, Thomas J, Pao VY, Nguyen TK, Levy HL, Greene C, Freehauf C, Chou JY. Methionine adenosyltransferase I/III deficiency: novel mutations and clinical variations. Am J Hum Genet. 2000 Feb;66(2):347-55. PMID:10677294 doi:10.1086/302752

2obv, resolution 2.05Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=2obv&oldid=3411325"