2obv: Difference between revisions

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[[Image:2obv.gif|left|200px]]


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==Crystal structure of the human S-adenosylmethionine synthetase 1 in complex with the product==
The line below this paragraph, containing "STRUCTURE_2obv", creates the "Structure Box" on the page.
<StructureSection load='2obv' size='340' side='right'caption='[[2obv]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<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>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.05&#8491;</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>
{{STRUCTURE_2obv| PDB=2obv |  SCENE= }}
<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>
== 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 ==
[https://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/main_output.php?pdb_ID=2obv ConSurf].
<div style="clear:both"></div>


'''Crystal structure of the human S-adenosylmethionine synthetase 1 in complex with the product'''
==See Also==
 
*[[Methionine adenosyltransferase|Methionine adenosyltransferase]]
 
*[[S-adenosylmethionine synthetase 3D structures|S-adenosylmethionine synthetase 3D structures]]
==About this Structure==
== References ==
2OBV is a [[Single protein]] structure of 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].
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Methionine adenosyltransferase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Arrowsmith CH]]
[[Category: Arrowsmith, C H.]]
[[Category: Cooper C]]
[[Category: Cooper, C.]]
[[Category: Edwards A]]
[[Category: Delft, F Von.]]
[[Category: Hozjan V]]
[[Category: Edwards, A.]]
[[Category: Kavanagh KL]]
[[Category: Hozjan, V.]]
[[Category: Oppermann U]]
[[Category: Kavanagh, K L.]]
[[Category: Pilka ES]]
[[Category: Oppermann, U.]]
[[Category: Shafqat N]]
[[Category: Pilka, E S.]]
[[Category: Sundstrom M]]
[[Category: SGC, Structural Genomics Consortium.]]
[[Category: Turnbull A]]
[[Category: Shafqat, N.]]
[[Category: Weigelt J]]
[[Category: Sundstrom, M.]]
[[Category: Von Delft F]]
[[Category: Turnbull, A.]]
[[Category: Weigelt, J.]]
[[Category: Sgc]]
[[Category: Structural genomic]]
[[Category: Structural genomics consortium]]
[[Category: Synthetase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 10:34:30 2008''

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

2obv 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 2.05Å
Ligands:, ,
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

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