Glutamate 83 and arginine 85 of helix H3 bend are key residues for FtsZ polymerization, GTPase activity and cellular viability of Escherichia coli: lateral mutations affect FtsZ polymerization and E. coli viability.
Shin, Jae Yen
Glutamate 83 and arginine 85 of helix H3 bend are key residues for FtsZ polymerization, GTPase activity and cellular viability of Escherichia coli: lateral mutations affect FtsZ polymerization and E. coli viability. [electronic resource] - BMC microbiology Feb 2013 - 26 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1471-2180
10.1186/1471-2180-13-26 doi
Amino Acid Sequence
Arginine--genetics
Bacterial Proteins--genetics
Cell Cycle Proteins--genetics
Cell Division
Cytoskeletal Proteins--genetics
Escherichia coli--enzymology
GTP Phosphohydrolases--metabolism
Glutamic Acid--genetics
Microbial Viability
Models, Molecular
Molecular Sequence Data
Mutant Proteins--genetics
Mutation, Missense
Protein Binding
Protein Conformation
Protein Interaction Mapping
Protein Multimerization
Glutamate 83 and arginine 85 of helix H3 bend are key residues for FtsZ polymerization, GTPase activity and cellular viability of Escherichia coli: lateral mutations affect FtsZ polymerization and E. coli viability. [electronic resource] - BMC microbiology Feb 2013 - 26 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1471-2180
10.1186/1471-2180-13-26 doi
Amino Acid Sequence
Arginine--genetics
Bacterial Proteins--genetics
Cell Cycle Proteins--genetics
Cell Division
Cytoskeletal Proteins--genetics
Escherichia coli--enzymology
GTP Phosphohydrolases--metabolism
Glutamic Acid--genetics
Microbial Viability
Models, Molecular
Molecular Sequence Data
Mutant Proteins--genetics
Mutation, Missense
Protein Binding
Protein Conformation
Protein Interaction Mapping
Protein Multimerization