1lt7
From Proteopedia
(New page: 200px<br /> <applet load="1lt7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lt7, resolution 2.15Å" /> '''Oxidized Homo sapie...) |
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caption="1lt7, resolution 2.15Å" /> | caption="1lt7, resolution 2.15Å" /> | ||
'''Oxidized Homo sapiens betaine-homocysteine S-methyltransferase in complex with four Sm(III) ions'''<br /> | '''Oxidized Homo sapiens betaine-homocysteine S-methyltransferase in complex with four Sm(III) ions'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LT7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SM and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Betaine--homocysteine_S-methyltransferase Betaine--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.5 2.1.1.5] Full crystallographic information is available from [http:// | + | 1LT7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SM:'>SM</scene> and <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Betaine--homocysteine_S-methyltransferase Betaine--homocysteine S-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.5 2.1.1.5] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT7 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:20:11 2008'' |
Revision as of 14:20, 15 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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