University at Buffalo - The State University of New York
Skip to Content
23940315[PMID] - PMC - NCBI

Display Settings:

Items per page

Search results

Items: 6

1.
Fig. 3.

Fig. 3. From: Cryoelectron tomography reveals the sequential assembly of bacterial flagella in Borrelia burgdorferi.

Intermediate structures of the flagellar rod. (AC) Three-dimensional maps of the ΔflgB, ΔflgC, and ΔflhO flagellar motors. (DF) Enlarged images of the regions outlined in (AC). In the ΔflgB mutant, the channel in the MS ring remains closed (D). In the ΔflgC mutant, the channel is in an open conformation, and a globular density is visible (E). In the ΔflhO mutant, the globular density is larger and extends beyond the MS ring (F). (GI) Three-dimensional surface rendering of the motors from the ΔflgB, ΔflgC, and ΔflhO mutants.

Xiaowei Zhao, et al. Proc Natl Acad Sci U S A. 2013 Aug 27;110(35):14390-14395.
2.
Fig. 4.

Fig. 4. From: Cryoelectron tomography reveals the sequential assembly of bacterial flagella in Borrelia burgdorferi.

Three-dimensional structures of the proximal rod and fully assembled rod. A central section (A) and 3D surface rendering (B) of the ΔflgG motor. A flanged tube structure is readily observed above the channel domain of the MS ring. (C) Three-dimensional surface rendering of the proximal rod. A central section (D) and 3D surface rendering (E) of the ΔflgE motor. The fully assembled rod, the P ring, and a cap structure (probably the hook cap) are revealed in E. (F) Three-dimensional surface rendering of the intact rod.

Xiaowei Zhao, et al. Proc Natl Acad Sci U S A. 2013 Aug 27;110(35):14390-14395.
3.
Fig. 2.

Fig. 2. From: Cryoelectron tomography reveals the sequential assembly of bacterial flagella in Borrelia burgdorferi.

The flagellar motor structure of the ΔfliE mutant reveals a closed conformation of the central channel. (A) Multiple flagellar motors are embedded in the inner membrane. Enlarged image (B) and 3D surface rendering (C) of the region outlined in A. A central section (D) and 3D surface rendering in top (E) and side (F) views of the ΔfliE motor. (G) A central channel domain (light green) is closed in the ΔfliE mutant. (H) Outline of the rod (orange) and the MS ring (green), and a 3D surface rendering (I) of the wild-type motor. The channel domain of the MS ring is in an open conformation, and the rod is assembled on top of the channel domain.

Xiaowei Zhao, et al. Proc Natl Acad Sci U S A. 2013 Aug 27;110(35):14390-14395.
4.
Fig. 5.

Fig. 5. From: Cryoelectron tomography reveals the sequential assembly of bacterial flagella in Borrelia burgdorferi.

Three-dimensional structures of the hook and the hook–filament junction. (A) Cryo-tomogram of a flaB mutant cell. The flagellar hook complex in two different orientations (B and C). The hook length is estimated to be ∼50 nm, and another ∼12 nm density is probably the hook–filament junction, as labeled in B and C. (D) Three-dimensional surface rendering of the flaB mutant flagellar structure. The hook (together with the hook–filament junction) and the filament cap are segmented. (E) Cryo-tomogram of a wild-type cell showing the flagellar motor with a hook and filament. (F and G) Three-dimensional structures of the flagellar hook and filament in wild-type cells. The diameter of the axial structure gradually becomes larger at the junction region. (H) Three-dimensional surface rendering of an intact flagellum.

Xiaowei Zhao, et al. Proc Natl Acad Sci U S A. 2013 Aug 27;110(35):14390-14395.
5.
Fig. 1.

Fig. 1. From: Cryoelectron tomography reveals the sequential assembly of bacterial flagella in Borrelia burgdorferi.

Structural differences between the intact flagellar motor and the purified flagella. (A) Model of a B. burgdorferi cell: outer membrane (OM), inner membrane (IM), and periplasmic flagella (PFs). (B and C) Models of a PF and an external flagellum. (D) A section from a wild-type cell tomogram. A central section (E) and an outline overlapping onto the map (F) of the intact motor. The MS ring is colored green, the rod and hook are colored orange, and the P ring (P), the export apparatus (EXP), the stator, and the collar are labeled accordingly. (G) A section from a purified PFs tomogram. A section (H) and an outline (I) of the basal body. The MS ring–rod complex remains in both the basal body (I) and the intact motor (F). (J) A 3D surface rendering of the intact motor (F).

Xiaowei Zhao, et al. Proc Natl Acad Sci U S A. 2013 Aug 27;110(35):14390-14395.
6.
Fig. 6.

Fig. 6. From: Cryoelectron tomography reveals the sequential assembly of bacterial flagella in Borrelia burgdorferi.

Modular architecture and assembly blueprint of bacterial flagella. (A) A model of flagellar assembly in B. burgdorferi. In the pre-T3S assembly state, many flagellar components assemble, including the MS ring, the C ring, the stators, the export apparatus, and the collar. The secretion channel in the MS ring is closed (first panel). In the presence of FliE and FlgB, rod substrates can be secreted but are unable to form a stable structure (second panel) until all of the proximal rod substrates (FliE, FlgB, FlgC, and FlhO) are present (third panel). The distal rod protein FlgG adds onto the proximal rod and polymerizes until it reaches a determined length (fourth panel). A hook cap composed of FlgD forms at the distal end of the rod (fourth panel) and promotes hook assembly (fifth panel). Assembly of the filament (FlaA and FlaB) is promoted by the filament cap (FliD) (sixth panel). (B) A cartoon model of a PF. Five rod proteins assemble sequentially on top of the channel domain of the MS ring and are enclosed by the socket domain of the MS ring and the P ring. The FlgG distal rod in the PF is shorter than that in the external flagellum (C). (D) A cartoon model of type III injectisome shows that the rod is anchored on a structure similar to the channel domain of the flagellar motor. The rod is a straight tube formed by one protein, PrgJ.

Xiaowei Zhao, et al. Proc Natl Acad Sci U S A. 2013 Aug 27;110(35):14390-14395.

Display Settings:

Items per page

Supplemental Content

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center