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通过X射线晶体学研究鸟苷二磷酸与大肠杆菌延伸因子Tu结合的结构细节。

Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography.

作者信息

la Cour T F, Nyborg J, Thirup S, Clark B F

出版信息

EMBO J. 1985 Sep;4(9):2385-8. doi: 10.1002/j.1460-2075.1985.tb03943.x.

DOI:10.1002/j.1460-2075.1985.tb03943.x
PMID:3908095
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC554514/
Abstract

Structural details of the guanosine diphosphate binding to a modified form of elongation factor Tu from Escherichia coli, resulting from X-ray crystallographic studies, are reported. The protein elements that take part in the nucleotide binding are located in four loops connecting beta-strands with alpha-helices. These loops correspond to regions in primary sequences which show a high degree of homology when compared with other prokaryotic and eukaryotic elongation factors and initiation factor 2.

摘要

报道了通过X射线晶体学研究得出的鸟苷二磷酸与大肠杆菌延伸因子Tu的一种修饰形式结合的结构细节。参与核苷酸结合的蛋白质元件位于连接β链与α螺旋的四个环中。这些环对应于与其他原核和真核延伸因子以及起始因子2相比在一级序列中显示出高度同源性的区域。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/684c/554514/c9d938be02af/emboj00274-0231-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/684c/554514/d4fc6035f4c0/emboj00274-0231-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/684c/554514/c9d938be02af/emboj00274-0231-b.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/684c/554514/d4fc6035f4c0/emboj00274-0231-a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/684c/554514/c9d938be02af/emboj00274-0231-b.jpg

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The primary structure of elongation factor G from Escherichia coli. A complete amino acid sequence.来自大肠杆菌的延伸因子G的一级结构。完整的氨基酸序列。
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