5dml: Difference between revisions
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''' | ==Crystal Structure of the Homocysteine Methyltransferase MmuM from Escherichia coli, Oxidized form== | ||
<StructureSection load='5dml' size='340' side='right' caption='[[5dml]], [[Resolution|resolution]] 2.45Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5dml]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DML OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DML 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></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dmn|5dmn]], [[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=5dml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dml OCA], [http://pdbe.org/5dml PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dml RCSB], [http://www.ebi.ac.uk/pdbsum/5dml 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 5dml" 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]] | ||
