2obv: Difference between revisions

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[[Image:2obv.gif|left|200px]]<br /><applet load="2obv" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2obv, resolution 2.05&Aring;" />
'''Crystal structure of the human S-adenosylmethionine synthetase 1 in complex with the product'''<br />


==Disease==
==Crystal structure of the human S-adenosylmethionine synthetase 1 in complex with the product==
Known diseases associated with this structure: Hypermethioninemia, persistent, autosomal dominant, due to methionine adenosyltransferase I/III deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=250850 250850]], Methionine adenosyltransferase deficiency, autosomal recessive OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=250850 250850]]
<StructureSection load='2obv' size='340' side='right'caption='[[2obv]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<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='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>
<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>


==About this Structure==
==See Also==
2OBV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NA:'>NA</scene>, <scene name='pdbligand=SAM:'>SAM</scene> and <scene name='pdbligand=PG4:'>PG4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OBV OCA].
*[[Methionine adenosyltransferase|Methionine adenosyltransferase]]
*[[S-adenosylmethionine synthetase 3D structures|S-adenosylmethionine synthetase 3D structures]]
== References ==
<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: NA]]
[[Category: PG4]]
[[Category: SAM]]
[[Category: sgc]]
[[Category: structural genomics]]
[[Category: structural genomics consortium]]
[[Category: synthetase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:16:40 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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