NMR backbone resonance assignment of New Delhi metallo-beta-lactamase.

作者: Chendie Yao , Qiong Wu , Guohua Xu , Conggang Li

DOI: 10.1007/S12104-017-9756-5

关键词:

摘要: The emerging of the New Delhi metallo-beta-lactamase (NDM-1) has become one greatest threats to clinical treatment. Although structure NDM-1 been determined by X-ray crystallography, molecular mechanism and process catalysis reaction remain elusive. NMR spectroscopy plays a unique role in characterization conformational dynamics. Here we report backbone 1H, 15N 13C chemical shift assignments heteronuclear multidimensional as well its secondary solution predicted TALOS+.

参考文章(13)
Mahesh Aitha, Abraham J. Moller, Indra D. Sahu, Masaki Horitani, David L. Tierney, Michael W. Crowder, Investigating the position of the hairpin loop in New Delhi metallo-β-lactamase, NDM-1, during catalysis and inhibitor binding Journal of Inorganic Biochemistry. ,vol. 156, pp. 35- 39 ,(2016) , 10.1016/J.JINORGBIO.2015.10.011
Pei W. Thomas, Min Zheng, Shanshan Wu, Hua Guo, Dali Liu, Dingguo Xu, Walter Fast, Characterization of Purified New Delhi Metallo-β-lactamase-1 Biochemistry. ,vol. 50, pp. 10102- 10113 ,(2011) , 10.1021/BI201449R
Min Zheng, Dingguo Xu, New Delhi metallo-β-lactamase I: substrate binding and catalytic mechanism. Journal of Physical Chemistry B. ,vol. 117, pp. 11596- 11607 ,(2013) , 10.1021/JP4065906
Youngchang Kim, Christine Tesar, Joseph Mire, Robert Jedrzejczak, Andrew Binkowski, Gyorgy Babnigg, James Sacchettini, Andrzej Joachimiak, Structure of Apo- and Monometalated Forms of NDM-1—A Highly Potent Carbapenem-Hydrolyzing Metallo-β-Lactamase PLoS ONE. ,vol. 6, pp. e24621- ,(2011) , 10.1371/JOURNAL.PONE.0024621
Victoria L. Green, Anil Verma, Raymond J. Owens, Simon E. V. Phillips, Stephen B. Carr, Structure of New Delhi metallo-β-lactamase 1 (NDM-1). Acta Crystallographica Section F-structural Biology and Crystallization Communications. ,vol. 67, pp. 1160- 1164 ,(2011) , 10.1107/S1744309111029654
Dustin King, Natalie Strynadka, Crystal structure of New Delhi metallo-β-lactamase reveals molecular basis for antibiotic resistance. Protein Science. ,vol. 20, pp. 1484- 1491 ,(2011) , 10.1002/PRO.697
Yu Guo, Jing Wang, Guojun Niu, Wenqing Shui, Yuna Sun, Honggang Zhou, Yaozhou Zhang, Cheng Yang, Zhiyong Lou, Zihe Rao, A structural view of the antibiotic degradation enzyme NDM-1 from a superbug Protein & Cell. ,vol. 2, pp. 384- 394 ,(2011) , 10.1007/S13238-011-1055-9
Karen Bush, Alarming β-lactamase-mediated resistance in multidrug-resistant Enterobacteriaceae. Current Opinion in Microbiology. ,vol. 13, pp. 558- 564 ,(2010) , 10.1016/J.MIB.2010.09.006
Yang Shen, Frank Delaglio, Gabriel Cornilescu, Ad Bax, TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. Journal of Biomolecular NMR. ,vol. 44, pp. 213- 223 ,(2009) , 10.1007/S10858-009-9333-Z
gMin Zhang, Quan Hao, Crystal structure of NDM-1 reveals a common β-lactam hydrolysis mechanism The FASEB Journal. ,vol. 25, pp. 2574- 2582 ,(2011) , 10.1096/FJ.11-184036