1lt7: Difference between revisions

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[[Image:1lt7.jpg|left|200px]]
{{Seed}}
[[Image:1lt7.png|left|200px]]


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{{STRUCTURE_1lt7|  PDB=1lt7  |  SCENE=  }}  
{{STRUCTURE_1lt7|  PDB=1lt7  |  SCENE=  }}  


'''Oxidized Homo sapiens betaine-homocysteine S-methyltransferase in complex with four Sm(III) ions'''
===Oxidized Homo sapiens betaine-homocysteine S-methyltransferase in complex with four Sm(III) ions===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_12220488}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_12220488}}


==About this Structure==
==About this Structure==
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[[Category: Transferase]]
[[Category: Transferase]]
[[Category: Zinc]]
[[Category: Zinc]]
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