1lt7
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Betaine-homocysteine methyl transferase (BHMT) catalyzes the synthesis of | + | Betaine-homocysteine methyl transferase (BHMT) catalyzes the synthesis of methionine from betaine and homocysteine (Hcy), utilizing a zinc ion to activate Hcy. BHMT is a key liver enzyme that is important for homocysteine homeostasis. X-ray structures of human BHMT in its oxidized (Zn-free) and reduced (Zn-replete) forms, the latter in complex with the bisubstrate analog, S(delta-carboxybutyl)-L-homocysteine, were determined at resolutions of 2.15 A and 2.05 A. BHMT is a (beta/alpha)(8) barrel that is distorted to construct the substrate and metal binding sites. The zinc binding sequences G-V/L-N-C and G-G-C-C are at the C termini of strands beta6 and beta8. Oxidation to the Cys217-Cys299 disulfide and expulsion of Zn are accompanied by local rearrangements. The structures identify Hcy binding fingerprints and provide a prototype for the homocysteine S-methyltransferase family. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Castro, C.]] | [[Category: Castro, C.]] | ||
| - | [[Category: Evans, J | + | [[Category: Evans, J C.]] |
| - | [[Category: Garrow, T | + | [[Category: Garrow, T A.]] |
| - | [[Category: Huddler, D | + | [[Category: Huddler, D P.]] |
[[Category: Jiracek, J.]] | [[Category: Jiracek, J.]] | ||
| - | [[Category: Ludwig, M | + | [[Category: Ludwig, M L.]] |
| - | [[Category: Millian, N | + | [[Category: Millian, N S.]] |
[[Category: CIT]] | [[Category: CIT]] | ||
[[Category: SM]] | [[Category: SM]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:12 2008'' |
Revision as of 11:48, 21 February 2008
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Oxidized Homo sapiens betaine-homocysteine S-methyltransferase in complex with four Sm(III) ions
Overview
Betaine-homocysteine methyl transferase (BHMT) catalyzes the synthesis of methionine from betaine and homocysteine (Hcy), utilizing a zinc ion to activate Hcy. BHMT is a key liver enzyme that is important for homocysteine homeostasis. X-ray structures of human BHMT in its oxidized (Zn-free) and reduced (Zn-replete) forms, the latter in complex with the bisubstrate analog, S(delta-carboxybutyl)-L-homocysteine, were determined at resolutions of 2.15 A and 2.05 A. BHMT is a (beta/alpha)(8) barrel that is distorted to construct the substrate and metal binding sites. The zinc binding sequences G-V/L-N-C and G-G-C-C are at the C termini of strands beta6 and beta8. Oxidation to the Cys217-Cys299 disulfide and expulsion of Zn are accompanied by local rearrangements. The structures identify Hcy binding fingerprints and provide a prototype for the homocysteine S-methyltransferase family.
About this Structure
1LT7 is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Betaine--homocysteine S-methyltransferase, with EC number 2.1.1.5 Full crystallographic information is available from OCA.
Reference
Betaine-homocysteine methyltransferase: zinc in a distorted barrel., Evans JC, Huddler DP, Jiracek J, Castro C, Millian NS, Garrow TA, Ludwig ML, Structure. 2002 Sep;10(9):1159-71. PMID:12220488
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