5dmn
From Proteopedia
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| - | ''' | + | ==Crystal Structure of the Homocysteine Methyltransferase MmuM from Escherichia coli, Apo form== |
| + | <StructureSection load='5dmn' size='340' side='right' caption='[[5dmn]], [[Resolution|resolution]] 2.89Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5dmn]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DMN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DMN FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dmm|5dmm]]</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Homocysteine_S-methyltransferase Homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.10 2.1.1.10] </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=5dmn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dmn OCA], [http://pdbe.org/5dmn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dmn RCSB], [http://www.ebi.ac.uk/pdbsum/5dmn PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/MMUM_ECOLI MMUM_ECOLI]] Catalyzes methyl transfer from S-methylmethionine or S-adenosylmethionine (less efficient) to homocysteine, selenohomocysteine and less efficiently selenocysteine.<ref>PMID:9882684</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Homocysteine S -methyltransferases (HMTs, EC 2.1.1.0) catalyze the conversion of homocysteine to methionine using S -methylmethionine or S -adenosylmethionine as the methyl donor. HMTs play an important role in methionine biosynthesis and are widely distributed among microorganisms, plants, and animals. Additionally, HMTs play a role in metabolite repair of S -adenosylmethionine by removing an inactive diastereomer from the pool. The mmuM gene product from Escherichia coli is an archetypal HMT family protein and contains a predicted Zn-binding motif in the enzyme active site. Here we present X-ray structures for MmuM in oxidized, apo, and metallated forms, representing the first such structures for any member of the HMT family. The structures reveal a metal/substrate binding pocket distinct from those in related enzymes. The presented structure analysis and modelling of co-substrate interactions provide valuable insight into the function of MmuM in both methionine biosynthesis and cofactor repair. | ||
| - | + | Crystal structure of the homocysteine methyltransferase MmuM from Escherichia coli.,Li K, Li G, Bradbury LM, Hanson AD, Bruner SD Biochem J. 2015 Nov 12. pii: BJ20150980. PMID:26564203<ref>PMID:26564203</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 5dmn" style="background-color:#fffaf0;"></div> | |
| - | [[Category: | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homocysteine S-methyltransferase]] | ||
| + | [[Category: Andrew, H D]] | ||
| + | [[Category: Bradbury, L M.T]] | ||
| + | [[Category: Bruner, S D]] | ||
| + | [[Category: Li, G]] | ||
[[Category: Li, K]] | [[Category: Li, K]] | ||
| - | [[Category: | + | [[Category: Homocysteine methyltransferase]] |
| - | [[Category: | + | [[Category: Transferase]] |
| - | + | ||
| - | + | ||
Revision as of 04:40, 1 December 2015
Crystal Structure of the Homocysteine Methyltransferase MmuM from Escherichia coli, Apo form
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