Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella

10.3791/58568 ◽  
2018 ◽  
Author(s):  
Bidhan Chandra Nayak ◽  
Jie Wang ◽  
Lianyun Lin ◽  
Weiyi He ◽  
Minsheng You ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ryanodine Receptor ◽  
Plutella Xylostella ◽  
Terminal Domain

Crystal structure of the N-terminal domain of ryanodine receptor from the honeybee, Apis mellifera

2020 ◽  
Vol 125 ◽  
pp. 103454
Author(s):  
Yuanyuan Zhou ◽  
Wenlan Wang ◽  
Nahiyan Mohammad Salauddin ◽  
Lianyun Lin ◽  
Minsheng You ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Apis Mellifera ◽  
Ryanodine Receptor ◽  
Terminal Domain

scholarly journals Author Correction: Crystal structure of Type IX secretion system PorE C-terminal domain from Porphyromonas gingivalis in complex with a peptidoglycan fragment

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Nhung Thi Trang Trinh ◽  
Hieu Quang Tran ◽  
Quyen Van Dong ◽  
Christian Cambillau ◽  
Alain Roussel ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Porphyromonas Gingivalis ◽  
Secretion System ◽  
Terminal Domain ◽  
Type Ix Secretion System

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

scholarly journals Crystal structure of the N-terminal domain of VqsR fromPseudomonas aeruginosaat 2.1 Å resolution

2017 ◽  
Vol 73 (7) ◽  
pp. 431-436
Author(s):  
Qing He ◽  
Kang Wang ◽  
Tiantian Su ◽  
Feng Wang ◽  
Lichuan Gu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Sequence Similarity ◽  
Transcriptional Regulator ◽  
Binding Domain ◽  
Structural Comparison ◽  
Homoserine Lactones ◽  
Terminal Domain ◽  
C Terminus ◽  
Common Motif ◽  
The Common

VqsR is a quorum-sensing (QS) transcriptional regulator which controls QS systems (las,rhlandpqs) by directly downregulating the expression ofqscRinPseudomonas aeruginosa. As a member of the LuxR family of proteins, VqsR shares the common motif of a helix–turn–helix (HTH)-type DNA-binding domain at the C-terminus, while the function of its N-terminal domain remains obscure. Here, the crystal structure of the N-terminal domain of VqsR (VqsR-N; residues 1–193) was determined at a resolution of 2.1 Å. The structure is folded into a regular α–β–α sandwich topology, which is similar to the ligand-binding domain (LBD) of the LuxR-type QS receptors. Although their sequence similarity is very low, structural comparison reveals that VqsR-N has a conserved enclosed cavity which could recognize acyl-homoserine lactones (AHLs) as in other LuxR-type AHL receptors. The structure suggests that VqsR could be a potential AHL receptor.

The 1.8-Å Crystal Structure of the N-Terminal Domain of an Archaeal MCM as a Right-Handed Filament

2014 ◽  
Vol 426 (7) ◽  
pp. 1512-1523 ◽  
Author(s):  
Yang Fu ◽  
Ian M. Slaymaker ◽  
Junfeng Wang ◽  
Ganggang Wang ◽  
Xiaojiang S. Chen
Keyword(s):  
Crystal Structure ◽  
Terminal Domain

scholarly journals Crystal Structure and Trimer-Monomer Transition of N-Terminal Domain of EhCaBP1 from Entamoeba histolytica

2010 ◽  
Vol 98 (12) ◽  
pp. 2933-2942 ◽  
Author(s):  
Shivesh Kumar ◽  
Ejaz Ahmad ◽  
M. Shahid Mansuri ◽  
Sanjeev Kumar ◽  
Ruchi Jain ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Entamoeba Histolytica ◽  
Terminal Domain
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