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-A 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.
Publication types
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Comparative Study
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Bacillus subtilis / chemistry*
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Bacillus subtilis / metabolism
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Bacterial Proteins / chemistry*
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Bacterial Proteins / physiology
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Crystallization
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Dimerization
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Histidine Kinase
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Models, Molecular
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Molecular Sequence Data
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Protein Folding
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Protein Kinases / metabolism
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Protein Structure, Tertiary
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Sequence Alignment
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Signal Transduction
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Structure-Activity Relationship
Substances
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Bacterial Proteins
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Protein Kinases
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Histidine Kinase