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空肠弯曲菌四环素抗性决定子Tet(O)推定的GTP结合结构域中Asn-128突变改变的影响

Effect of mutational alteration of Asn-128 in the putative GTP-binding domain of tetracycline resistance determinant Tet(O) from Campylobacter jejuni.

作者信息

Grewal J, Manavathu E K, Taylor D E

机构信息

Department of Medical Microbiology and Infectious Diseases, University of Alberta, Edmonton, Canada.

出版信息

Antimicrob Agents Chemother. 1993 Dec;37(12):2645-9. doi: 10.1128/AAC.37.12.2645.

DOI:10.1128/AAC.37.12.2645
PMID:8109930
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC192766/
Abstract

The deduced amino acid sequence of Campylobacter jejuni Tet(O), cloned in Escherichia coli, has shown that it contains the five highly conserved sequences of the GTP-binding domain found in other GTPases. Asn-128 belongs to the G4 motif of such a domain and is involved in hydrogen bonding with the guanine ring of the nucleotide. Substitution of Asn-128 by 11 other amino acids resulted in a decrease in tetracycline resistance, indicating that tetracycline resistance conferred by Tet(O) is related to GTP binding. The effect of the mutations on the GTP-binding domain is discussed with the EF-Tu-GDP complex as a model.

摘要

空肠弯曲杆菌Tet(O)在大肠杆菌中克隆后的推导氨基酸序列表明，它含有在其他GTP酶中发现的GTP结合结构域的五个高度保守序列。Asn-128属于该结构域的G4基序，参与与核苷酸鸟嘌呤环的氢键形成。用其他11种氨基酸取代Asn-128导致四环素抗性降低，表明Tet(O)赋予的四环素抗性与GTP结合有关。以EF-Tu-GDP复合物为模型讨论了这些突变对GTP结合结构域的影响。

相似文献

1
Effect of mutational alteration of Asn-128 in the putative GTP-binding domain of tetracycline resistance determinant Tet(O) from Campylobacter jejuni.空肠弯曲菌四环素抗性决定子Tet(O)推定的GTP结合结构域中Asn-128突变改变的影响
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2
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