A dimeric two-component receiver domain inhibits the sigma54-dependent ATPase in DctD

FASEB J. 2001 May;15(7):1326-8. doi: 10.1096/fj.00-0516fje.

Authors

M G Meyer¹, S Park, L Zeringue, M Staley, M McKinstry, R I Kaufman, H Zhang, D Yan, N Yennawar, H Yennawar, G K Farber, B T Nixon

Affiliation

¹ Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.

PMID: 11344129
DOI: 10.1096/fj.00-0516fje

No abstract available

MeSH terms

Adenosine Triphosphatases / genetics
Adenosine Triphosphatases / metabolism*
Bacterial Proteins / chemistry
Bacterial Proteins / genetics
Bacterial Proteins / metabolism*
Crystallography, X-Ray
DNA-Binding Proteins*
DNA-Directed RNA Polymerases / metabolism*
Dimerization
Phosphorylation
Protein Structure, Tertiary*
RNA Polymerase Sigma 54
Sigma Factor / metabolism*
Signal Transduction / physiology*
Transcription Factors / chemistry
Transcription Factors / genetics
Transcription Factors / metabolism*

Substances

Bacterial Proteins
DNA-Binding Proteins
Sigma Factor
Transcription Factors
dctD protein, Rhizobium meliloti
DNA-Directed RNA Polymerases
RNA Polymerase Sigma 54
Adenosine Triphosphatases