1lt8: Difference between revisions
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[[Image:1lt8.jpg|left|200px]] | [[Image:1lt8.jpg|left|200px]] | ||
'''Reduced Homo sapiens Betaine-Homocysteine S-Methyltransferase in Complex with S-(delta-carboxybutyl)-L-Homocysteine''' | {{Structure | ||
|PDB= 1lt8 |SIZE=350|CAPTION= <scene name='initialview01'>1lt8</scene>, resolution 2.05Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=CBH:S-(D-CARBOXYBUTYL)-L-HOMOCYSTEINE'>CBH</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= | |||
}} | |||
'''Reduced Homo sapiens Betaine-Homocysteine S-Methyltransferase in Complex with S-(delta-carboxybutyl)-L-Homocysteine''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LT8 is a [ | 1LT8 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=1LT8 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 12:34:56 2008'' | ||
Revision as of 13:34, 20 March 2008
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| , resolution 2.05Å | |||||||
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| Ligands: | , and | ||||||
| Activity: | Betaine--homocysteine S-methyltransferase, with EC number 2.1.1.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Reduced Homo sapiens Betaine-Homocysteine S-Methyltransferase in Complex with S-(delta-carboxybutyl)-L-Homocysteine
OverviewOverview
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 StructureAbout this Structure
1LT8 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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