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| | <StructureSection load='5dml' size='340' side='right'caption='[[5dml]], [[Resolution|resolution]] 2.45Å' scene=''> | | <StructureSection load='5dml' size='340' side='right'caption='[[5dml]], [[Resolution|resolution]] 2.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5dml]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. 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> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dmn|5dmn]], [[5dmm|5dmm]]</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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mmuM, yagD, b0261, JW0253 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</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> |
| - | <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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5dml ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Homocysteine S-methyltransferase]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Andrew, H D]] | + | [[Category: Andrew HD]] |
| - | [[Category: Bradbury, L M.T]] | + | [[Category: Bradbury LMT]] |
| - | [[Category: Bruner, S D]] | + | [[Category: Bruner SD]] |
| - | [[Category: Li, G]] | + | [[Category: Li G]] |
| - | [[Category: Li, K]] | + | [[Category: Li K]] |
| - | [[Category: Homocysteine methyltransferase]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
MMUM_ECOLI Catalyzes methyl transfer from S-methylmethionine or S-adenosylmethionine (less efficient) to homocysteine, selenohomocysteine and less efficiently selenocysteine.[1]
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Thanbichler M, Neuhierl B, Bock A. S-methylmethionine metabolism in Escherichia coli. J Bacteriol. 1999 Jan;181(2):662-5. PMID:9882684
- ↑ Li K, Li G, Bradbury LM, Hanson AD, Bruner SD. Crystal structure of the homocysteine methyltransferase MmuM from Escherichia coli. Biochem J. 2015 Nov 12. pii: BJ20150980. PMID:26564203 doi:http://dx.doi.org/10.1042/BJ20150980
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