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.
Blanchard, John S.
中科院分区:
生物学1区
文献类型:
--
作者:
Vetting, Matthew W.;Hegde, Subray S.;Blanchard, John S.

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结核分枝杆菌酶 Rv2275 使用两分子 Tyr-tRNATyr 作为底物催化环 (L-Tyr-L-Tyr) 的形成。 Rv2275 的三维结构确定为 2.0 Å 分辨率,表明 Rv2275 在结构上与 Ic 类氨酰基-tRNA 合成酶家族相关。诱变和放射性标记表明存在一种共价中间体,其中 L-酪氨酸通过酯交换作用从 Tyr-tRNATyr 转移到活性位点丝氨酸 (S88),并且 E233 作为催化二肽键形成的关键碱基。
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.
DOI: 10.1074/jbc.m301565200
发表时间: 2003-06-20
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期刊: NATURE STRUCTURAL BIOLOGY
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