The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase.
The structure and mechanism of the Mycobacterium tuberculosis cyclodityrosine synthetase.
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DOI:
10.1038/nchembio.440
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发表时间:
2010-11
影响因子:
14.8
通讯作者:
Blanchard, John S.
中科院分区:
文献类型:
--
作者:
Vetting, Matthew W.;Hegde, Subray S.;Blanchard, John S.
The Mycobacterium tuberculosis enzyme Rv2275 catalyzes the formation of cyclo(L-Tyr-L-Tyr) using two molecules of Tyr-tRNATyr as substrates. The three-dimensional structure of Rv2275 was determined to 2.0 Å resolution, revealing that Rv2275 is structurally related to the class Ic aminoacyl-tRNA-synthetase family of enzymes. Mutagenesis and radioactive labeling suggests a covalent intermediate in which L-tyrosine is transferred from Tyr-tRNATyr to an active site serine (S88) by transesterification and with E233 serving as a critical base catalyzing dipeptide bond formation.
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影响因子:
4.8
作者:
Hegde, SS;Blanchard, JS
通讯作者:
Blanchard, JS
DOI:
10.1038/nsb934
发表时间:
2003-06-01
期刊:
NATURE STRUCTURAL BIOLOGY
影响因子:
--
作者:
Kobayashi, T;Nureki, O;Yokoyama, S
通讯作者:
Yokoyama, S
影响因子:
1.6
作者:
Kanoh, K;Kohno, S;Uno, I
通讯作者:
Uno, I
影响因子:
14.8
作者:
Gondry, Muriel;Sauguet, Ludovic;Pernodet, Jean-Luc
通讯作者:
Pernodet, Jean-Luc
DOI:
10.1107/s0907444904026460
发表时间:
2004-12-01
影响因子:
2.2
作者:
Krissinel, E;Henrick, K
通讯作者:
Henrick, K