1x1c | pdb_00001x1c
Crystal structure of BchU complexed with S-adenosyl-L-homocysteine and Zn2+
Structural highlights
FunctionBCHU_CHLTE Involved in the biosynthesis of the major light-harvesting pigment bacteriochlorophyll c (BChlc), which confers a significant competitive advantage to green sulfur bacteria living at limiting red and near-infrared light intensities (PubMed:15090495). Catalyzes the methylation at the C-20 position of the cyclic tetrapyrrole chlorin of bacteriochlorophyll d (BChld) to produce bacteriochlorophyll c (BChlc) using S-adenosylmethionine (SAM) as a methyl source (PubMed:15090495, PubMed:16797589).[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedBchU plays a role in bacteriochlorophyll c biosynthesis by catalyzing methylation at the C-20 position of cyclic tetrapyrrole chlorin using S-adenosylmethionine (SAM) as a methyl source. This methylation causes red-shifts of the electronic absorption spectrum of the light-harvesting pigment, allowing green photosynthetic bacteria to adapt to low-light environments. We have determined the crystal structures of BchU and its complex with S-adenosylhomocysteine (SAH). BchU forms a dimer and each subunit consists of two domains, an N-terminal domain and a C-terminal domain. Dimerization occurs through interactions between the N-terminal domains and the residues responsible for the catalytic reaction are in the C-terminal domain. The binding site of SAH is located in a large cavity between the two domains, where SAH is specifically recognized by many hydrogen bonds and a salt-bridge. The electron density map of BchU in complex with an analog of bacteriochlorophyll c located its central metal near the SAH-binding site, but the tetrapyrrole ring was invisible, suggesting that binding of the ring to BchU is loose and/or occupancy of the ring is low. It is likely that His290 acts as a ligand for the central metal of the substrate. The orientation of the substrate was predicted by simulation, and allows us to propose a mechanism for the BchU directed methylation: the strictly conserved Tyr246 residue acts catalytically in the direct transfer of the methyl group from SAM to the substrate through an S(N)2-like mechanism. Crystal structures of BchU, a methyltransferase involved in bacteriochlorophyll c biosynthesis, and its complex with S-adenosylhomocysteine: implications for reaction mechanism.,Wada K, Yamaguchi H, Harada J, Niimi K, Osumi S, Saga Y, Oh-Oka H, Tamiaki H, Fukuyama K J Mol Biol. 2006 Jul 21;360(4):839-49. Epub 2006 Jun 8. PMID:16797589[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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