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本文引用的文献

1
Suppressor mutations in Escherichia coli methionyl-tRNA formyltransferase: role of a 16-amino acid insertion module in initiator tRNA recognition.大肠杆菌甲硫氨酰 - tRNA甲酰转移酶中的抑制突变：16个氨基酸插入模块在起始tRNA识别中的作用。
Proc Natl Acad Sci U S A. 1997 Dec 9;94(25):13524-9. doi: 10.1073/pnas.94.25.13524.
2
Cross-validated maximum likelihood enhances crystallographic simulated annealing refinement.交叉验证的最大似然法增强了晶体学模拟退火精修。
Proc Natl Acad Sci U S A. 1997 May 13;94(10):5018-23. doi: 10.1073/pnas.94.10.5018.
3
Lysine 207 as the site of cross-linking between the 3'-end of Escherichia coli initiator tRNA and methionyl-tRNA formyltransferase.赖氨酸207作为大肠杆菌起始tRNA 3'末端与甲硫氨酰-tRNA甲酰基转移酶之间的交联位点。
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Molecular recognition governing the initiation of translation in Escherichia coli. A review.大肠杆菌中控制翻译起始的分子识别。综述。
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Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase.结晶态大肠杆菌甲硫氨酰 - tRNA(f)Met甲酰基转移酶的结构：与甘氨酰胺核糖核苷酸甲酰基转移酶的比较。
EMBO J. 1996 Sep 2;15(17):4749-58.
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Interplay of methionine tRNAs with translation elongation factor Tu and translation initiation factor 2 in Escherichia coli.大肠杆菌中甲硫氨酸tRNA与翻译延伸因子Tu及翻译起始因子2的相互作用
J Biol Chem. 1996 Sep 13;271(37):22321-5. doi: 10.1074/jbc.271.37.22321.
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Crystallization and preliminary X-ray analysis of Escherichia coli methionyl-tRNA(fMet) formyltransferase.大肠杆菌甲硫氨酰 - tRNA（fMet）甲酰基转移酶的结晶及初步X射线分析。
Proteins. 1996 May;25(1):139-41. doi: 10.1002/prot.14.
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Role of the three consecutive G:C base pairs conserved in the anticodon stem of initiator tRNAs in initiation of protein synthesis in Escherichia coli.起始tRNA反密码子茎中保守的三个连续G:C碱基对在大肠杆菌蛋白质合成起始中的作用。
RNA. 1996 May;2(5):473-82.
9
Important role of the amino acid attached to tRNA in formylation and in initiation of protein synthesis in Escherichia coli.附着于tRNA的氨基酸在大肠杆菌甲酰化及蛋白质合成起始过程中的重要作用。
J Biol Chem. 1996 Jan 12;271(2):1022-8. doi: 10.1074/jbc.271.2.1022.
10
SETOR: hardware-lighted three-dimensional solid model representations of macromolecules.SETOR：大分子的硬件照明三维实体模型表示
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甲硫氨酰 - tRNAfMet转甲酰基酶与起始甲酰甲硫氨酰 - tRNAfMet复合物的晶体结构。

Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet.

作者信息

Schmitt E, Panvert M, Blanquet S, Mechulam Y

机构信息

Laboratoire de Biochimie, Unité Mixte de Recherche No. 7654 du Centre National de la Recherche Scientifique, Ecole Polytechnique, F-91128 Palaiseau cedex, France.

出版信息

EMBO J. 1998 Dec 1;17(23):6819-26. doi: 10.1093/emboj/17.23.6819.

DOI:10.1093/emboj/17.23.6819
PMID:9843487
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1171029/
Abstract

The crystal structure of Escherichia coli methionyl-tRNAfMet transformylase complexed with formyl-methionyl-tRNAfMet was solved at 2.8 A resolution. The formylation reaction catalyzed by this enzyme irreversibly commits methionyl-tRNAfMet to initiation of translation in eubacteria. In the three-dimensional model, the methionyl-tRNAfMet formyltransferase fills in the inside of the L-shaped tRNA molecule on the D-stem side. The anticodon stem and loop are away from the protein. An enzyme loop is wedged in the major groove of the acceptor helix. As a result, the C1-A72 mismatch characteristic of the initiator tRNA is split and the 3' arm bends inside the active centre. This recognition mechanism is markedly distinct from that of elongation factor Tu, which binds the acceptor arm of aminoacylated elongator tRNAs on the T-stem side.

摘要

以2.8埃的分辨率解析了与甲酰甲硫氨酰 - tRNAfMet复合的大肠杆菌甲硫氨酰 - tRNAfMet转甲酰酶的晶体结构。该酶催化的甲酰化反应不可逆地使甲硫氨酰 - tRNAfMet参与真细菌的翻译起始。在三维模型中，甲硫氨酰 - tRNAfMet转甲酰酶填充在L形tRNA分子D茎侧的内部。反密码子茎环远离蛋白质。一个酶环楔入受体螺旋的大沟中。结果，起始tRNA特有的C1 - A72错配被分开，3'臂在活性中心内弯曲。这种识别机制与延伸因子Tu的识别机制明显不同，延伸因子Tu在T茎侧结合氨酰化延伸tRNA的受体臂。