Mutational analysis of charged residues in the putative KdpB-TM5 domain of the Kdp-ATPase of Escherichia coli

Ann N Y Acad Sci. 2003 Apr:986:351-3. doi: 10.1111/j.1749-6632.2003.tb07213.x.

Authors

Marc Bramkamp¹, Karlheinz Altendorf

Affiliation

¹ Universität Osnabrück, Fachbereich Biologie/Chemie, Abteilung Mikrobiologie, Germany. [email protected]

PMID: 12763849
DOI: 10.1111/j.1749-6632.2003.tb07213.x

No abstract available

MeSH terms

Adenosine Triphosphatases / chemistry*
Adenosine Triphosphatases / genetics
Adenosine Triphosphatases / metabolism*
Amino Acid Sequence
Amino Acid Substitution
Binding Sites
Cation Transport Proteins / chemistry*
Cation Transport Proteins / genetics
Cation Transport Proteins / metabolism*
Escherichia coli / enzymology*
Escherichia coli / genetics
Escherichia coli Proteins / chemistry*
Escherichia coli Proteins / genetics
Escherichia coli Proteins / metabolism*
Kinetics
Models, Molecular
Mutagenesis, Site-Directed
Operon*
Protein Structure, Secondary
Recombinant Proteins / chemistry
Recombinant Proteins / metabolism

Substances

Cation Transport Proteins
Escherichia coli Proteins
Recombinant Proteins
Adenosine Triphosphatases
potassium translocating Kdp-ATPase, E coli