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在无锌和锌(II)结合状态下,同二聚体锌传感器AdcR(32 kDa)的主链和立体特异性甲基侧链共振归属。

Backbone and sterospecific methyl side chain resonance assignments of the homodimeric zinc sensor AdcR (32 kDa) in the apo- and Zn(II)-bound states.

作者信息

Guerra Alfredo J, Giedroc David P

机构信息

Department of Chemistry, Indiana University, Bloomington, IN, 47405-7102, USA.

出版信息

Biomol NMR Assign. 2014 Apr;8(1):11-4. doi: 10.1007/s12104-012-9442-6. Epub 2012 Nov 9.

Abstract

Streptococcus pneumoniae adhesin competence repressor (AdcR) is a Zn(II)-dependent 32 kDa homodimer that controls the transcription of a zinc-specific ABC uptake system (AdcABC), three pneumococcal histidine triad proteins (PhtA, PhtD and PhtE), and an AdcA homolog AdcAII. AdcR is the first metal-dependent member of the MarR family of prokaryotic transcriptional repressors. Two-dimensional NMR studies reveal large changes in the spectrum upon Zn(II) binding. Near complete backbone and stereospecific methyl group resonance assignments for apo- and Zn(II)-AdcR are presented here.

摘要

肺炎链球菌黏附素感受态阻遏蛋白(AdcR)是一种依赖锌(II)的32 kDa同型二聚体,它控制着锌特异性ABC摄取系统(AdcABC)、三种肺炎球菌组氨酸三联体蛋白(PhtA、PhtD和PhtE)以及AdcA同源物AdcAII的转录。AdcR是原核转录阻遏蛋白MarR家族中第一个依赖金属的成员。二维核磁共振研究揭示了锌(II)结合后光谱的巨大变化。本文给出了脱辅基和锌(II)-AdcR近乎完整的主链和立体特异性甲基基团共振归属。

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