scholarly journals The Crystal Structure of Bacillus subtilis YycI Reveals a Common Fold for Two Members of an Unusual Class of Sensor Histidine Kinase Regulatory Proteins

2007 ◽  
Vol 189 (8) ◽  
pp. 3290-3295 ◽  
Author(s):  
Eugenio Santelli ◽  
Robert C. Liddington ◽  
Michael A. Mohan ◽  
James A. Hoch ◽  
Hendrik Szurmant
Keyword(s):  
Crystal Structure ◽  
Bacillus Subtilis ◽  
Sequence Homology ◽  
Histidine Kinase ◽  
Direct Interaction ◽  
Regulatory Proteins ◽  
Sensor Histidine Kinase ◽  
Periplasmic Proteins ◽  
Terminal Domains

ABSTRACT YycI and YycH are two membrane-anchored periplasmic proteins that regulate the essential Bacillus subtilis YycG histidine kinase through direct interaction. Here we present the crystal structure of YycI at a 2.9-Å resolution. YycI forms a dimer, and remarkably the structure resembles that of the two C-terminal domains of YycH despite nearly undetectable sequence homology (10%) between the two proteins.

scholarly journals Insight into the sporulation phosphorelay: Crystal structure of the sensor domain of Bacillus subtilis histidine kinase, KinD

2013 ◽  
Vol 22 (5) ◽  
pp. 564-576 ◽  
Author(s):  
R. Wu ◽  
M. Gu ◽  
R. Wilton ◽  
G. Babnigg ◽  
Y. Kim ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Bacillus Subtilis ◽  
Histidine Kinase ◽  
Insight Into

scholarly journals 1P-260 The Photoreaction of the PYP Domain in the Light Sensor Histidine Kinase Ppr is Influenced by the C-terminal Domains(The 46th Annual Meeting of the Biophysical Society of Japan)

2008 ◽  
Vol 48 (supplement) ◽  
pp. S62
Author(s):  
Hironari Kamikubo ◽  
Tomonori Koyama ◽  
Michihiro Hayashi ◽  
Kumiko Shirai ◽  
Yoichi Yamazaki ◽  
...  
Keyword(s):  
Annual Meeting ◽  
Histidine Kinase ◽  
Sensor Histidine Kinase ◽  
Light Sensor ◽  
Biophysical Society ◽  
Terminal Domains

scholarly journals The Crystal Structure of Beryllofluoride Spo0F in Complex with the Phosphotransferase Spo0B Represents a Phosphotransfer Pretransition State

2006 ◽  
Vol 188 (13) ◽  
pp. 4970-4977 ◽  
Author(s):  
Kottayil I. Varughese ◽  
Igor Tsigelny ◽  
Haiyan Zhao
Keyword(s):  
Crystal Structure ◽  
Bacillus Subtilis ◽  
Transition State ◽  
Histidine Kinase ◽  
In Silico ◽  
Phosphoryl Group ◽  
Phosphoryl Transfer ◽  
Regulatory Circuits ◽  
Phosphoryl Groups ◽  
In Silico Models

ABSTRACT A number of regulatory circuits in biological systems function through the exchange of phosphoryl groups from one protein to another. Spo0F and Spo0B are components of a phosphorelay that control sporulation in the bacterium Bacillus subtilis through the exchange of a phosphoryl group. Using beryllofluoride as a mimic for phosphorylation, we trapped the interaction of the phosphorylated Spo0F with Spo0B in the crystal lattice. The transition state of phosphoryl transfer continues to be a highly debated issue, as to whether it is associative or dissociative in nature. The geometry of Spo0F binding to Spo0B favors an associative mechanism for phosphoryl transfer. In order to visualize the autophosphorylation of the histidine kinase, KinA, and the subsequent phosphoryl transfer to Spo0F, we generated in silico models representing these reaction steps.

The Photoreaction of the Photoactive Yellow Protein Domain in the Light Sensor Histidine Kinase Ppr is Influenced by the C-terminal Domains

2008 ◽  
Vol 84 (4) ◽  
pp. 895-902 ◽  
Author(s):  
Hironari Kamikubo ◽  
Tomonori Koyama ◽  
Michihiro Hayashi ◽  
Kumiko Shirai ◽  
Yoichi Yamazaki ◽  
...  
Keyword(s):  
Histidine Kinase ◽  
Protein Domain ◽  
Photoactive Yellow Protein ◽  
Sensor Histidine Kinase ◽  
Light Sensor ◽  
Terminal Domains

scholarly journals Extracytoplasmic PAS-Like Domains Are Common in Signal Transduction Proteins

2009 ◽  
Vol 192 (4) ◽  
pp. 1156-1159 ◽  
Author(s):  
Changsoo Chang ◽  
Christine Tesar ◽  
Minyi Gu ◽  
Gyorgy Babnigg ◽  
Andrzej Joachimiak ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Signal Transduction ◽  
Histidine Kinase ◽  
Pas Domain ◽  
Two Component System ◽  
Component System ◽  
Sensor Histidine Kinase ◽  
Two Component ◽  
Sensor Kinases ◽  
Signal Transduction Proteins

ABSTRACT We present the crystal structure of the extracytoplasmic domain of the Bacillus subtilis PhoR sensor histidine kinase, part of a two-component system involved in adaptation to low environmental phosphate concentrations. In addition to the PhoR structure, we predict that the majority of the extracytoplasmic domains of B. subtilis sensor kinases will adopt a fold similar to the ubiquitous PAS domain.

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