5dmm

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==Crystal Structure of the Homocysteine Methyltransferase MmuM from Escherichia coli, Metallated form==
==Crystal Structure of the Homocysteine Methyltransferase MmuM from Escherichia coli, Metallated form==
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<StructureSection load='5dmm' size='340' side='right' caption='[[5dmm]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
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<StructureSection load='5dmm' size='340' side='right'caption='[[5dmm]], [[Resolution|resolution]] 1.78&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5dmm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DMM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5DMM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5dmm]] 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=5DMM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DMM FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.779&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5dmn|5dmn]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=HCS:2-AMINO-4-MERCAPTO-BUTYRIC+ACID'>HCS</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5dmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dmm OCA], [https://pdbe.org/5dmm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5dmm RCSB], [https://www.ebi.ac.uk/pdbsum/5dmm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5dmm ProSAT]</span></td></tr>
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<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=5dmm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dmm OCA], [http://pdbe.org/5dmm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dmm RCSB], [http://www.ebi.ac.uk/pdbsum/5dmm PDBsum]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[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>
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[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>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5dmm" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Homocysteine S-methyltransferase]]
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[[Category: Escherichia coli K-12]]
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[[Category: Andrew, H D]]
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[[Category: Large Structures]]
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[[Category: Bradbury, L M.T]]
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[[Category: Andrew HD]]
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[[Category: Bruner, S D]]
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[[Category: Bradbury LMT]]
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[[Category: Li, G]]
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[[Category: Bruner SD]]
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[[Category: Li, K]]
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[[Category: Li G]]
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[[Category: Homocysteine methyltransferase]]
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[[Category: Li K]]
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[[Category: Transferase]]
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Current revision

Crystal Structure of the Homocysteine Methyltransferase MmuM from Escherichia coli, Metallated form

PDB ID 5dmm

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