5ZIY

Crystal structure of Bacillus cereus FlgL

Summary for 5ZIY

• Entry DOI: 10.2210/pdb5ziy/pdb
• Descriptor: Flagellar hook-associated protein 3, ZINC ION (3 entities in total)
• Functional Keywords: flagellum, junction, structural protein
• Biological source: Bacillus cereus
• Total number of polymer chains: 2
• Total formula weight: 47712.53

Authors

Hong, H.J.,Kim, T.H.,Song, W.S.,Yoon, S.I. (deposition date: 2018-03-18, release date: 2018-10-17, Last modification date: 2024-03-27)

Primary citation

Hong, H.J.,Kim, T.H.,Song, W.S.,Ko, H.J.,Lee, G.S.,Kang, S.G.,Kim, P.H.,Yoon, S.I.
Crystal structure of FlgL and its implications for flagellar assembly
Sci Rep, 8:14307-14307, 2018

PubMed Abstract: Bacteria move toward attractants and away from repellants by rotating their flagellum. The bacterial flagellum assembles through the ordered organization of more than 30 different proteins. Among the diverse flagellar proteins, FlgL forms the junction between the hook and the filament in the flagellum together with FlgK and provides a structural base where flagellin, a filament-forming protein, is inserted for the initiation of filament elongation. However, the functional and structural information available for FlgL is highly limited. To provide structural insights into the cross-linkage between the FlgL junction and the flagellin filament, we determined the crystal structures of FlgL from gram-positive Bacillus cereus (bcFlgL) and gram-negative Xanthomonas campestris (xcFlgL). bcFlgL contains one domain (D1), whereas xcFlgL adopts a two-domain structure that consists of the D1 and D2 domains. The constant D1 domain of FlgL adopts a rod structure that is generated by four longitudinal segments. This four-segment structure is recapitulated in filament and junction proteins but not in hook and rod proteins, allowing us to propose a junction-filament assembly mechanism based on a quasi-homotypic interaction. The D2 domain of xcFlgL resembles that of another junction protein, FlgK, suggesting the structural and functional relatedness of FlgL and FlgK.

PubMed: 30250171
DOI: 10.1038/s41598-018-32460-9

Experimental method

X-RAY DIFFRACTION (2.2 Å)