5dml
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==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 with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5DML 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]] 2.452Å</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></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=5dml FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dml OCA], [https://pdbe.org/5dml PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dml RCSB], [https://www.ebi.ac.uk/pdbsum/5dml PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dml ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://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> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5dml" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Andrew HD]] | ||
| + | [[Category: Bradbury LMT]] | ||
| + | [[Category: Bruner SD]] | ||
| + | [[Category: Li G]] | ||
| + | [[Category: Li K]] | ||
Current revision
Crystal Structure of the Homocysteine Methyltransferase MmuM from Escherichia coli, Oxidized form
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