1lt7
From Proteopedia
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|PDB= 1lt7 |SIZE=350|CAPTION= <scene name='initialview01'>1lt7</scene>, resolution 2.15Å | |PDB= 1lt7 |SIZE=350|CAPTION= <scene name='initialview01'>1lt7</scene>, resolution 2.15Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</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] | + | |ACTIVITY= <span class='plainlinks'>[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] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1lt8|1lt8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lt7 OCA], [http://www.ebi.ac.uk/pdbsum/1lt7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lt7 RCSB]</span> | ||
}} | }} | ||
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[[Category: Ludwig, M L.]] | [[Category: Ludwig, M L.]] | ||
[[Category: Millian, N S.]] | [[Category: Millian, N S.]] | ||
| - | [[Category: CIT]] | ||
| - | [[Category: SM]] | ||
[[Category: homocysteine metabolism]] | [[Category: homocysteine metabolism]] | ||
[[Category: homocysteinemia]] | [[Category: homocysteinemia]] | ||
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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 Sun Mar 30 22:07:05 2008'' |
Revision as of 19:07, 30 March 2008
| |||||||
| , resolution 2.15Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Betaine--homocysteine S-methyltransferase, with EC number 2.1.1.5 | ||||||
| Related: | 1lt8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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