Structure of the response regulator ChrA in the haem-sensing two-component system of Corynebacterium diphtheriae

被引：5
|
作者：
Doi, Akihiro [1 ]
Nakamura, Hiro [1 ]
Shiro, Yoshitsugu [1 ]
Sugimoto, Hiroshi [1 ]
机构：
[1] RIKEN SPring 8 Ctr, Sayo, Hyogo 6795148, Japan
来源：
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2015年 / 71卷
关键词：
transcription factor; X-ray crystallography; haem; helix-turn-helix; phosphorylation; SIGNAL-TRANSDUCTION SYSTEM; CONFORMATIONAL-CHANGES; RECEIVER DOMAIN; GENE-EXPRESSION; IRON SOURCES; NARL; PHOSPHORYLATION; ACTIVATION; IDENTIFICATION; HEMOGLOBIN;
D O I：
10.1107/S2053230X15009838
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
ChrA is a response regulator (RR) in the two-component system involved in regulating the degradation and transport of haem (Fe-porphyrin) in the pathogen Corynebacterium diphtheriae. Here, the crystal structure of full-length ChrA is described at a resolution of 1.8 angstrom. ChrA consists of an N-terminal regulatory domain, a long linker region and a C-terminal DNA-binding domain. A structural comparison of ChrA with other RRs revealed substantial differences in the relative orientation of the two domains and the conformation of the linker region. The structural flexibility of the linker could be an important feature in rearrangement of the domain orientation to create a dimerization interface to bind DNA during haem-sensing signal transduction.
引用
收藏
页码：966 / 971
页数：6
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