4ccz

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{{STRUCTURE_4ccz| PDB=4ccz | SCENE= }}
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==Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains==
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===Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains===
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<StructureSection load='4ccz' size='340' side='right' caption='[[4ccz]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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==Disease==
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<table><tr><td colspan='2'>[[4ccz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CCZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CCZ 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=THG:(6S)-5,6,7,8-TETRAHYDROFOLATE'>THG</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/Methionine_synthase Methionine synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.13 2.1.1.13] </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=4ccz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ccz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ccz RCSB], [http://www.ebi.ac.uk/pdbsum/4ccz PDBsum]</span></td></tr>
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</table>
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== Disease ==
[[http://www.uniprot.org/uniprot/METH_HUMAN METH_HUMAN]] Defects in MTR are the cause of methylcobalamin deficiency type G (cblG) [MIM:[http://omim.org/entry/250940 250940]]; also known as homocystinuria-megaloblastic anemia complementation type G. It is an autosomal recessive inherited disease that causes mental retardation, macrocytic anemia, and homocystinuria. Mild deficiency in MS activity could be associated with mild hyperhomocysteinemia, a risk factor for cardiovascular disease and possibly neural tube defects. MS mutations could also be involved in tumorigenesis. Defects in MTR may be a cause of susceptibility to folate-sensitive neural tube defects (FS-NTD) [MIM:[http://omim.org/entry/601634 601634]]. The most common NTDs are open spina bifida (myelomeningocele) and anencephaly. Genetic defects in MTR may affect the risk of spina bifida via the maternal rather than the embryonic genotype.<ref>PMID:12375236</ref> <ref>PMID:15979034</ref>
[[http://www.uniprot.org/uniprot/METH_HUMAN METH_HUMAN]] Defects in MTR are the cause of methylcobalamin deficiency type G (cblG) [MIM:[http://omim.org/entry/250940 250940]]; also known as homocystinuria-megaloblastic anemia complementation type G. It is an autosomal recessive inherited disease that causes mental retardation, macrocytic anemia, and homocystinuria. Mild deficiency in MS activity could be associated with mild hyperhomocysteinemia, a risk factor for cardiovascular disease and possibly neural tube defects. MS mutations could also be involved in tumorigenesis. Defects in MTR may be a cause of susceptibility to folate-sensitive neural tube defects (FS-NTD) [MIM:[http://omim.org/entry/601634 601634]]. The most common NTDs are open spina bifida (myelomeningocele) and anencephaly. Genetic defects in MTR may affect the risk of spina bifida via the maternal rather than the embryonic genotype.<ref>PMID:12375236</ref> <ref>PMID:15979034</ref>
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== Function ==
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==Function==
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[[http://www.uniprot.org/uniprot/METH_HUMAN METH_HUMAN]] Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity).
[[http://www.uniprot.org/uniprot/METH_HUMAN METH_HUMAN]] Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate (By similarity).
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== References ==
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==About this Structure==
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<references/>
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[[4ccz]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CCZ OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Human]]
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<references group="xtra"/><references/>
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[[Category: Methionine synthase]]
[[Category: Methionine synthase]]
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[[Category: Arrowsmith, C.]]
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[[Category: Arrowsmith, C]]
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[[Category: Bountra, C.]]
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[[Category: Bountra, C]]
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[[Category: Burgess-Brown, N.]]
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[[Category: Burgess-Brown, N]]
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[[Category: Delft, F von.]]
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[[Category: Delft, F von]]
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[[Category: Edwards, A.]]
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[[Category: Edwards, A]]
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[[Category: Goubin, S.]]
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[[Category: Goubin, S]]
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[[Category: Kiyani, W.]]
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[[Category: Kiyani, W]]
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[[Category: Krojer, T.]]
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[[Category: Krojer, T]]
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[[Category: Oppermann, U.]]
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[[Category: Oppermann, U]]
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[[Category: Vollmar, M.]]
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[[Category: Vollmar, M]]
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[[Category: Yue, W W.]]
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[[Category: Yue, W W]]
[[Category: Transferase]]
[[Category: Transferase]]

Revision as of 17:02, 21 December 2014

Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains

4ccz, resolution 2.70Å

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