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1lt7
From Proteopedia
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| - | [[Image:1lt7.jpg|left|200px]] | + | [[Image:1lt7.jpg|left|200px]] |
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| - | '''Oxidized Homo sapiens betaine-homocysteine S-methyltransferase in complex with four Sm(III) ions''' | + | {{Structure |
| + | |PDB= 1lt7 |SIZE=350|CAPTION= <scene name='initialview01'>1lt7</scene>, resolution 2.15Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene> and <scene name='pdbligand=CIT:CITRIC ACID'>CIT</scene> | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Oxidized Homo sapiens betaine-homocysteine S-methyltransferase in complex with four Sm(III) ions''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LT7 is a [ | + | 1LT7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LT7 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/12220488 12220488] |
[[Category: Betaine--homocysteine S-methyltransferase]] | [[Category: Betaine--homocysteine S-methyltransferase]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:34:55 2008'' |
Revision as of 10:34, 20 March 2008
| |||||||
| , resolution 2.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Activity: | Betaine--homocysteine S-methyltransferase, with EC number 2.1.1.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 12:34:55 2008
