Characterization of the nucleotide-binding domain NsrF from the BceAB-type ABC-transporter NsrFP from the human pathogen Streptococcus agalactiae

被引：9
|
作者：
Furtmann, Fabia [1 ]
Porta, Nicola [2 ]
Hoang, Dai Tri [1 ]
Reiners, Jens [3 ]
Schumacher, Julia [1 ]
Gottstein, Julia [1 ]
Gohlke, Holger [2 ,4 ]
Smits, Sander H. J. [1 ,3 ]
机构：
[1] Heinrich Heine Univ Dusseldorf, Inst Biochem, Univ Str 1, D-40225 Dusseldorf, Germany
[2] Heinrich Heine Univ Dusseldorf, Inst Pharmaceut & Med Chem, Univ Str 1, D-40225 Dusseldorf, Germany
[3] Heinrich Heine Univ Dusseldorf, Ctr Struct Studies, Univ Str 1, D-40225 Dusseldorf, Germany
[4] Forschungszentrum Julich, Inst Biol Informat Proc IBI 7 Struct Biochem, Inst Biol Informat Proc, John von Neumann Inst Comp NIC,Julich Supercomp C, Wilhelm Johnen Str, D-52425 Julich, Germany
来源：
SCIENTIFIC REPORTS | 2020年 / 10卷 / 01期
关键词：
SMALL-ANGLE SCATTERING; ATP-BINDING; MOLECULAR-DYNAMICS; ESCHERICHIA-COLI; HEMOLYSIN-B; LIPID-II; STAPHYLOCOCCUS-AUREUS; SIGNATURE SEQUENCE; RESISTANCE; PROTEIN;
D O I：
10.1038/s41598-020-72237-7
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
Treatment of bacterial infections is a great challenge of our era due to the various resistance mechanisms against antibiotics. Antimicrobial peptides are considered to be potential novel compound as antibiotic treatment. However, some bacteria, especially many human pathogens, are inherently resistant to these compounds, due to the expression of BceAB-type ABC transporters. This rather new transporter family is not very well studied. Here, we report the first full characterization of the nucleotide binding domain of a BceAB type transporter from Streptococcus agalactiae, namely SaNsrF of the transporter SaNsrFP, which confers resistance against nisin and gallidermin. We determined the NTP hydrolysis kinetics and used molecular modeling and simulations in combination with small angle X-ray scattering to obtain structural models of the SaNsrF monomer and dimer. The fact that the SaNsrF(H202A) variant displayed no ATPase activity was rationalized in terms of changes of the structural dynamics of the dimeric interface. Kinetic data show a clear preference for ATP as a substrate, and the prediction of binding modes allowed us to explain this selectivity over other NTPs.
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页数：16
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