Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex.
Insights into pyrrolysine function from structures of a trimethylamine methyltransferase and its corrinoid protein complex.
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DOI:
10.1038/s42003-022-04397-3
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发表时间:
2023-01-16
影响因子:
5.9
通讯作者:
中科院分区:
文献类型:
--
作者:
The 22nd genetically encoded amino acid, pyrrolysine, plays a unique role in the key step in the growth of methanogens on mono-, di-, and tri-methylamines by activating the methyl group of these substrates for transfer to a corrinoid cofactor. Previous crystal structures of the Methanosarcina barkeri monomethylamine methyltransferase elucidated the structure of pyrrolysine and provide insight into its role in monomethylamine activation. Herein, we report the second structure of a pyrrolysine-containing protein, the M. barkeri trimethylamine methyltransferase MttB, and its structure bound to sulfite, a substrate analog of trimethylamine. We also report the structure of MttB in complex with its cognate corrinoid protein MttC, which specifically receives the methyl group from the pyrrolysine-activated trimethylamine substrate during methanogenesis. Together these structures provide key insights into the role of pyrrolysine in methyl group transfer from trimethylamine to the corrinoid cofactor in MttC. Structures of Methanosarcina barkeri trimethylamine methyltransferase (MttB) with its substrates reveal the role of pyrrolysine in methyl group transfer from trimethylamine to the corrinoid cofactor in MttC.
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DOI:
10.1107/s0907444905036693
发表时间:
2006-01-01
影响因子:
2.2
作者:
Evans, P
通讯作者:
Evans, P
影响因子:
12.2
作者:
Brugère JF;Borrel G;Gaci N;Tottey W;O'Toole PW;Malpuech-Brugère C
通讯作者:
Malpuech-Brugère C
DOI:
10.1107/s0907444904019158
发表时间:
2004-12-01
影响因子:
2.2
作者:
Emsley, P;Cowtan, K
通讯作者:
Cowtan, K
影响因子:
56.9
作者:
DRENNAN, CL;HUANG, S;LUDWIG, ML
通讯作者:
LUDWIG, ML
影响因子:
30.8
作者:
GISH, W;STATES, DJ
通讯作者:
STATES, DJ