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2e0k
From Proteopedia
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[[Image:2e0k.jpg|left|200px]] | [[Image:2e0k.jpg|left|200px]] | ||
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'''Crystal structure of CbiL, a methyltransferase involved in anaerobic vitamin B12 biosynthesis''' | '''Crystal structure of CbiL, a methyltransferase involved in anaerobic vitamin B12 biosynthesis''' | ||
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Crystal structures of CbiL, a methyltransferase involved in anaerobic vitamin B biosynthesis, and CbiL in complex with S-adenosylhomocysteine--implications for the reaction mechanism., Wada K, Harada J, Yaeda Y, Tamiaki H, Oh-Oka H, Fukuyama K, FEBS J. 2007 Jan;274(2):563-73. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17229157 17229157] | Crystal structures of CbiL, a methyltransferase involved in anaerobic vitamin B biosynthesis, and CbiL in complex with S-adenosylhomocysteine--implications for the reaction mechanism., Wada K, Harada J, Yaeda Y, Tamiaki H, Oh-Oka H, Fukuyama K, FEBS J. 2007 Jan;274(2):563-73. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17229157 17229157] | ||
[[Category: Chlorobaculum tepidum]] | [[Category: Chlorobaculum tepidum]] | ||
| - | [[Category: Precorrin-2 C(20)-methyltransferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fukuyama, K.]] | [[Category: Fukuyama, K.]] | ||
[[Category: Wada, K.]] | [[Category: Wada, K.]] | ||
| - | [[Category: | + | [[Category: Cobalt-factor ii]] |
| - | [[Category: | + | [[Category: Precorrin-2]] |
| - | [[Category: | + | [[Category: S-adenosylmethionine]] |
| - | [[Category: | + | [[Category: Tetrapyrrole]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 01:42:39 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 22:42, 3 May 2008
Crystal structure of CbiL, a methyltransferase involved in anaerobic vitamin B12 biosynthesis
Overview
During anaerobic cobalamin (vitamin B12) biosynthesis, CbiL catalyzes methylation at the C-20 position of a cyclic tetrapyrrole ring using S-adenosylmethionine as a methyl group source. This methylation is a key modification for the ring contraction process, by which a porphyrin-type tetrapyrrole ring is converted to a corrin ring through elimination of the modified C-20 and direct bonding of C-1 to C-19. We have determined the crystal structures of Chlorobium tepidum CbiL and CbiL in complex with S-adenosylhomocysteine (the S-demethyl form of S-adenosylmethionine). CbiL forms a dimer in the crystal, and each subunit consists of N-terminal and C-terminal domains. S-Adenosylhomocysteine binds to a cleft between the two domains, where it is specifically recognized by extensive hydrogen bonding and van der Waals interactions. The orientation of the cobalt-factor II substrate was modeled by simulation, and the predicted model suggests that the hydroxy group of Tyr226 is located in close proximity to the C-20 atom as well as the C-1 and C-19 atoms of the tetrapyrrole ring. These configurations allow us to propose a catalytic mechanism: the conserved Tyr226 residue in CbiL catalyzes the direct transfer of a methyl group from S-adenosylmethionine to the substrate through an S(N)2-like mechanism. Furthermore, the structural model of CbiL binding to its substrate suggests the axial residue coordinated to the central cobalt of cobalt-factor II.
About this Structure
2E0K is a Single protein structure of sequence from Chlorobaculum tepidum. Full crystallographic information is available from OCA.
Reference
Crystal structures of CbiL, a methyltransferase involved in anaerobic vitamin B biosynthesis, and CbiL in complex with S-adenosylhomocysteine--implications for the reaction mechanism., Wada K, Harada J, Yaeda Y, Tamiaki H, Oh-Oka H, Fukuyama K, FEBS J. 2007 Jan;274(2):563-73. PMID:17229157 Page seeded by OCA on Sun May 4 01:42:39 2008
