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Nucleic Acids Res. 2000 Dec 1;28(23):4611-6. doi: 10.1093/nar/28.23.4611.
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Processing of X-ray diffraction data collected in oscillation mode.振荡模式下收集的X射线衍射数据的处理。
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Molden: a pre- and post-processing program for molecular and electronic structures.Molden：一款用于分子和电子结构的预处理和后处理程序。
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RNA aptamers for the MS2 bacteriophage coat protein and the wild-type RNA operator have similar solution behaviour.针对MS2噬菌体外壳蛋白和野生型RNA操纵子的RNA适体具有相似的溶液行为。
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Crystallographic studies of RNA hairpins in complexes with recombinant MS2 capsids: implications for binding requirements.与重组MS2衣壳形成复合物的RNA发夹的晶体学研究：对结合要求的启示
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Crystal structures of a series of RNA aptamers complexed to the same protein target.一系列与同一蛋白质靶标复合的RNA适配体的晶体结构。
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Crystallography & NMR system: A new software suite for macromolecular structure determination.晶体学与核磁共振系统：用于大分子结构测定的新软件套件。
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7
NMR structure and dynamics of an RNA motif common to the spliceosome branch-point helix and the RNA-binding site for phage GA coat protein.剪接体分支点螺旋和噬菌体GA外壳蛋白RNA结合位点共有的RNA基序的核磁共振结构与动力学
Biochemistry. 1998 Sep 29;37(39):13486-98. doi: 10.1021/bi981558a.
8
A thermodynamic analysis of the sequence-specific binding of RNA by bacteriophage MS2 coat protein.噬菌体MS2外壳蛋白与RNA序列特异性结合的热力学分析。
Proc Natl Acad Sci U S A. 1998 Aug 4;95(16):9244-9. doi: 10.1073/pnas.95.16.9244.
9
Crystal structures of MS2 coat protein mutants in complex with wild-type RNA operator fragments.与野生型RNA操纵片段复合的MS2外壳蛋白突变体的晶体结构。
Nucleic Acids Res. 1998 Mar 1;26(5):1345-51. doi: 10.1093/nar/26.5.1345.
10
Crystal structure of an RNA aptamer-protein complex at 2.8 A resolution.RNA适配体-蛋白质复合物的晶体结构，分辨率为2.8埃。
Nat Struct Biol. 1998 Feb;5(2):133-9. doi: 10.1038/nsb0298-133.

从MS2 RNA操纵基因中删除单个氢键原子会导致RNA-外壳蛋白界面处发生显著重排。

Deletion of a single hydrogen bonding atom from the MS2 RNA operator leads to dramatic rearrangements at the RNA-coat protein interface.

作者信息

Grahn E, Stonehouse N J, Adams C J, Fridborg K, Beigelman L, Matulic-Adamic J, Warriner S L, Stockley P G, Liljas L

机构信息

Department of Cell and Molecular Biology, Uppsala University, Box 596, SE-751 24 Uppsala, Sweden.

出版信息

Nucleic Acids Res. 2000 Dec 1;28(23):4611-6. doi: 10.1093/nar/28.23.4611.

DOI:10.1093/nar/28.23.4611
PMID:11095669
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC115176/
Abstract

The MS2 coat protein binds specifically to an RNA hairpin formed within the viral genome. By soaking different RNA fragments into crystals of MS2 coat protein capsids it is possible to determine the X-ray structure of the RNA-protein complexes formed. Here we present the structure to 2.85 A resolution of a complex between a chemically modified RNA hairpin variant and the MS2 coat protein. This RNA variant has a substitution at the -5 base position, which has been shown previously to be pyrimidine-specific and is a uracil in the wild-type RNA. The modified RNA hairpin contains a pyridin-4-one base (4one) at this position that lacks the exocyclic 2-oxygen eliminating the possibility of forming a hydrogen bond to asparagine A87 in the protein. The 4one complex structure shows an unprecedented major conformational change in the loop region of the RNA, whereas there is almost no change in the conformation of the protein.

摘要

MS2外壳蛋白特异性结合病毒基因组内形成的RNA发夹结构。通过将不同的RNA片段浸泡到MS2外壳蛋白衣壳晶体中，就有可能确定所形成的RNA-蛋白质复合物的X射线结构。在此，我们展示了化学修饰的RNA发夹变体与MS2外壳蛋白之间复合物的结构，分辨率达到2.85埃。这种RNA变体在-5碱基位置有一个取代，先前已证明该位置对嘧啶具有特异性，在野生型RNA中是尿嘧啶。修饰后的RNA发夹在该位置含有一个吡啶-4-酮碱基（4one），其缺少环外2-氧，消除了与蛋白质中天冬酰胺A87形成氢键的可能性。4one复合物结构显示RNA环区域出现了前所未有的主要构象变化，而蛋白质的构象几乎没有变化。