2e0n
From Proteopedia
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|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> | |LIGAND= <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene> | ||
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Precorrin-2_C(20)-methyltransferase Precorrin-2 C(20)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.130 2.1.1.130] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Precorrin-2_C(20)-methyltransferase Precorrin-2 C(20)-methyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.1.1.130 2.1.1.130] </span> |
|GENE= cbiL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1097 Chlorobaculum tepidum]) | |GENE= cbiL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1097 Chlorobaculum tepidum]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2e0k|2E0K]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2e0n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2e0n OCA], [http://www.ebi.ac.uk/pdbsum/2e0n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2e0n RCSB]</span> | ||
}} | }} | ||
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[[Category: Fukuyama, K.]] | [[Category: Fukuyama, K.]] | ||
[[Category: Wada, K.]] | [[Category: Wada, K.]] | ||
| - | [[Category: SAH]] | ||
[[Category: cobalt-factor ii]] | [[Category: cobalt-factor ii]] | ||
[[Category: precorrin-2]] | [[Category: precorrin-2]] | ||
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[[Category: tetrapyrrole]] | [[Category: tetrapyrrole]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:42:01 2008'' |
Revision as of 23:42, 30 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | cbiL (Chlorobaculum tepidum) | ||||||
| Activity: | Precorrin-2 C(20)-methyltransferase, with EC number 2.1.1.130 | ||||||
| Related: | 2E0K
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of CbiL in complex with S-adenosylhomocysteine, 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
2E0N 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
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