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==Crystal Structure of S-Adenosylmethionine synthetase (MetK/Mat) from Cryptosporidium parvum== | ==Crystal Structure of S-Adenosylmethionine synthetase (MetK/Mat) from Cryptosporidium parvum== | ||
<StructureSection load='6c07' size='340' side='right' caption='[[6c07]], [[Resolution|resolution]] 1.85Å' scene=''> | <StructureSection load='6c07' size='340' side='right'caption='[[6c07]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6c07]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C07 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6c07]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Cryptosporidium_parvum_Iowa_II Cryptosporidium parvum Iowa II]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C07 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6c07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c07 OCA], [https://pdbe.org/6c07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c07 RCSB], [https://www.ebi.ac.uk/pdbsum/6c07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c07 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/Q5CYE4_CRYPI Q5CYE4_CRYPI] Catalyzes the formation of S-adenosylmethionine from methionine and ATP.[RuleBase:RU000541] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
S-Adenosyl-L-methionine (AdoMet), the primary methyl donor in most biological methylation reactions, is produced from ATP and methionine in a multistep reaction catalyzed by AdoMet synthetase. The diversity of group-transfer reactions that involve AdoMet places this compound at a key crossroads in amino-acid, nucleic acid and lipid metabolism, and disruption of its synthesis has adverse consequences for all forms of life. The family of AdoMet synthetases is highly conserved, and structures of this enzyme have been determined from organisms ranging from bacteria to humans. Here, the structure of an AdoMet synthetase from the infectious parasite Cryptosporidium parvum has been determined as part of an effort to identify structural differences in this enzyme family that can guide the development of species-selective inhibitors. This enzyme form has a less extensive subunit interface than some previously determined structures, and contains some key structural differences from the human enzyme in an allosteric site, presenting an opportunity for the design of selective inhibitors against the AdoMet synthetase from this organism. | |||
Structure of a critical metabolic enzyme: S-adenosylmethionine synthetase from Cryptosporidium parvum.,Ohren J, Parungao GG, Viola RE Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):290-298. doi:, 10.1107/S2053230X19002772. Epub 2019 Apr 2. PMID:30950830<ref>PMID:30950830</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6c07" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[S-adenosylmethionine synthetase 3D structures|S-adenosylmethionine synthetase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Cryptosporidium parvum Iowa II]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Ohren JF]] | ||
[[Category: | [[Category: Viola RE]] | ||
Latest revision as of 17:53, 4 October 2023
Crystal Structure of S-Adenosylmethionine synthetase (MetK/Mat) from Cryptosporidium parvumCrystal Structure of S-Adenosylmethionine synthetase (MetK/Mat) from Cryptosporidium parvum
Structural highlights
FunctionQ5CYE4_CRYPI Catalyzes the formation of S-adenosylmethionine from methionine and ATP.[RuleBase:RU000541] Publication Abstract from PubMedS-Adenosyl-L-methionine (AdoMet), the primary methyl donor in most biological methylation reactions, is produced from ATP and methionine in a multistep reaction catalyzed by AdoMet synthetase. The diversity of group-transfer reactions that involve AdoMet places this compound at a key crossroads in amino-acid, nucleic acid and lipid metabolism, and disruption of its synthesis has adverse consequences for all forms of life. The family of AdoMet synthetases is highly conserved, and structures of this enzyme have been determined from organisms ranging from bacteria to humans. Here, the structure of an AdoMet synthetase from the infectious parasite Cryptosporidium parvum has been determined as part of an effort to identify structural differences in this enzyme family that can guide the development of species-selective inhibitors. This enzyme form has a less extensive subunit interface than some previously determined structures, and contains some key structural differences from the human enzyme in an allosteric site, presenting an opportunity for the design of selective inhibitors against the AdoMet synthetase from this organism. Structure of a critical metabolic enzyme: S-adenosylmethionine synthetase from Cryptosporidium parvum.,Ohren J, Parungao GG, Viola RE Acta Crystallogr F Struct Biol Commun. 2019 Apr 1;75(Pt 4):290-298. doi:, 10.1107/S2053230X19002772. Epub 2019 Apr 2. PMID:30950830[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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