Structure of the Escherichia coli response regulator NarL

The crystal structure analysis of the NarL protein provides a first look at interactions between receiver and effector domains of a full-length bacterial response regulator. The N-terminal receiver domain, with 131 amino acids, is folded into a 5-strand beta sheet flanked by 5 alpha helices, as seen...

Celý popis

Uložené v:
Podrobná bibliografia
Vydané v:Biochemistry (Easton) Ročník 35; číslo 34; s. 11053
Hlavní autori: Baikalov, I, Schröder, I, Kaczor-Grzeskowiak, M, Grzeskowiak, K, Gunsalus, R P, Dickerson, R E
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: United States 27.08.1996
Predmet:
Amino Acid Sequence
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Binding Sites
Crystallography, X-Ray
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - metabolism
Escherichia coli - chemistry
Escherichia coli Proteins
Models, Molecular
Molecular Sequence Data
Phosphorylation
Protein Conformation
Protein Structure, Secondary
Recombinant Proteins - chemistry
Repressor Proteins
Sequence Alignment
Trans-Activators
ISSN:0006-2960
On-line prístup:Zistit podrobnosti o prístupe
Tagy: Pridať tag
Žiadne tagy, Buďte prvý, kto otaguje tento záznam!
Popis
Shrnutí:The crystal structure analysis of the NarL protein provides a first look at interactions between receiver and effector domains of a full-length bacterial response regulator. The N-terminal receiver domain, with 131 amino acids, is folded into a 5-strand beta sheet flanked by 5 alpha helices, as seen in CheY and in the N-terminal domain of NTRC. The C-terminal DNA-binding domain, with 62 amino acids, is a compact bundle of 4 alpha helices, of which the middle 2 form a helix-turn-helix motif closely related to that of Drosophila paired protein and other H-T-H DNA-binding proteins. The 2 domains are connected by an alpha helix of 10 amino acids and a 13-residue flexible tether that is not visible and presumably disordered in the X-ray structure. In this unphosphorylated form of NarL, the C-terminal domain is turned against the receiver domain in a manner that would preclude DNA binding. Activation of NarL via phosphorylation of Asp59 must involve transfer of information to the interdomain interface and either rotation or displacement of the DNA-binding C-terminal domain. Docking of a B-DNA duplex against the isolated C-terminal domain in the manner observed in paired protein and other H-T-H proteins suggests a stereochemical basis for DNA sequence preference: T-R-C-C-Y (high affinity) or T-R-C-T-N (low affinity), which is close to the experimentally observed consensus sequence: T-A-C-Y-N. The NarL structure is a model for other members of the FixJ or LuxR family of bacterial transcriptional activators, and possibly to the more distant OmpR and NtrC families as well.
Bibliografia:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-2960
DOI:10.1021/bi960919o