Domain organization of flagellar hook protein from Salmonella typhimurium.


Abstract

Hook forms a universal joint, which mediates the torque of the flagellar motor to the outer helical filaments. Domain organization of hook protein from Salmonella typhimurium was investigated by exploring thermal denaturation properties of its proteolytic fragments. The most stable part of hook protein involves residues 148 to 355 and consists of two domains, as revealed by deconvolution analysis of the calorimetric melting profiles. Residues 72-147 and 356-370 form another domain, while the terminal regions of the molecule, residues 1-71 and 371-403, avoid a compact tertiary structure in the monomeric state. These folding domains were assigned to the morphological domains of hook subunits known from EM image reconstructions, revealing the overall folding of hook protein in its filamentous state. Study holds ProTherm entries: 5513, 5514, 6052, 6053, 6054, 6055, 6056 Extra Details: bacterial flagellum; hook; domain structure; calorimetry;,Salmonella typhimurium

Submission Details

ID: z9JCskAy

Submitter: Connie Wang

Submission Date: April 24, 2018, 8:30 p.m.

Version: 1

Publication Details
Uedaira H;Morii H;Ishimura M;Taniguchi H;Namba K;Vonderviszt F,FEBS Lett. (1999) Domain organization of flagellar hook protein from Salmonella typhimurium. PMID:10069386
Additional Information

Structure view and single mutant data analysis

Study data

No weblogo for data of varying length.
Colors: D E R H K S T N Q A V I L M F Y W C G P
 

Data Distribution

Studies with similar sequences (approximate matches)

Correlation with other assays (exact sequence matches)


Relevant PDB Entries

Structure ID Release Date Resolution Structure Title
1WLG 2004-11-02 1.8 Crystal structure of FlgE31, a major fragment of the hook protein
3A69 2009-12-15 7.1 Atomic model of the bacterial flagellar hook based on docking an X-ray derived structure and terminal two alpha-helices into an 7.1 angstrom resolution cryoEM map
2BGY 2005-01-27 9.0 Fit of the x-ray strucutre of the baterial flagellar hook fragment flge31 into an EM map from the hook of Caulobacter crescentus.
2BGZ 2005-01-27 9.0 ATOMIC MODEL OF THE BACTERIAL FLAGELLAR BASED ON DOCKING AN X-RAY DERIVED HOOK STRUCTURE INTO AN EM MAP.

Relevant UniProtKB Entries

Percent Identity Matching Chains Protein Accession Entry Name
100.0 Flagellar hook protein FlgE P0A1J1 FLGE_SALTY
100.0 Flagellar hook protein FlgE P0A1J2 FLGE_SALTI