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通过同核和异核核磁共振对溶液中大肠杆菌素E9免疫蛋白的二级结构元件进行顺序归属和鉴定。

Sequential assignments and identification of secondary structure elements of the colicin E9 immunity protein in solution by homonuclear and heteronuclear NMR.

作者信息

Osborne M J, Lian L Y, Wallis R, Reilly A, James R, Kleanthous C, Moore G R

机构信息

Schools of Chemical and Biological Sciences, University of East Anglia, Norwich, U.K.

出版信息

Biochemistry. 1994 Oct 18;33(41):12347-55. doi: 10.1021/bi00207a001.

DOI:10.1021/bi00207a001
PMID:7918457
Abstract

1H-1H, 1H-15N, and 1H-1H-15N multidimensional NMR spectroscopic studies of the 86 amino acid protein that provides immunity against the DNase action of colicin E9 are reported. Through a combination of 2D NOESY and TOCSY and 3D TOCSY-HMQC, NOESY-HMQC, and HMQC-NOESY-HMQC experiments, almost complete 1H NMR and backbone 15N NMR assignments have been obtained, and the secondary structure of the protein has been partially elucidated. Approximately 50% of the protein forms three helices. The specificity determining region of the DNase immunity protein, identified from previously reported biochemical studies to include residues 32-40, is helical, indicating that the protein-protein interaction involves residues from at least one helix.

摘要

报道了对一种86个氨基酸的蛋白质进行的1H-1H、1H-15N和1H-1H-15N多维核磁共振光谱研究，该蛋白质可抵御大肠杆菌素E9的脱氧核糖核酸酶作用。通过二维核Overhauser效应光谱（NOESY）和全相关光谱（TOCSY）以及三维TOCSY-异核多量子相干（HMQC）、NOESY-HMQC和HMQC-NOESY-HMQC实验的结合，几乎完成了1H核磁共振和主链15N核磁共振归属，并部分阐明了该蛋白质的二级结构。大约50%的蛋白质形成三个螺旋。从先前报道的生化研究中确定的脱氧核糖核酸酶免疫蛋白的特异性决定区域包括32 - 40位残基，该区域呈螺旋状，表明蛋白质 - 蛋白质相互作用涉及至少一个螺旋的残基。

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引用本文的文献

1
NMR investigation of the interaction of the inhibitor protein Im9 with its partner DNase.抑制剂蛋白Im9与其伴侣脱氧核糖核酸酶相互作用的核磁共振研究。
Protein Sci. 2000 Sep;9(9):1709-18. doi: 10.1110/ps.9.9.1709.
2
NMR detection of slow conformational dynamics in an endonuclease toxin.核酸内切酶毒素中缓慢构象动力学的核磁共振检测
J Biomol NMR. 1998 Jul;12(1):145-59. doi: 10.1023/a:1008272928173.
3
A structural comparison of the colicin immunity proteins Im7 and Im9 gives new insights into the molecular determinants of immunity-protein specificity.
大肠杆菌素免疫蛋白Im7和Im9的结构比较为免疫蛋白特异性的分子决定因素提供了新见解。
Biochem J. 1998 Jul 1;333 ( Pt 1)(Pt 1):183-91. doi: 10.1042/bj3330183.
4
Identification of critical residues in the colicin E9 DNase binding region of the Im9 protein.鉴定Im9蛋白的大肠杆菌素E9脱氧核糖核酸酶结合区域中的关键残基。
Biochem J. 1997 May 1;323 ( Pt 3)(Pt 3):823-31. doi: 10.1042/bj3230823.
5
The crystal structure of the immunity protein of colicin E7 suggests a possible colicin-interacting surface.大肠杆菌素E7免疫蛋白的晶体结构表明存在一个可能与大肠杆菌素相互作用的表面。
Proc Natl Acad Sci U S A. 1996 Jun 25;93(13):6437-42. doi: 10.1073/pnas.93.13.6437.