High-resolution crystal structure of an outer membrane-anchored endolytic peptidoglycan lytic transglycosylase (MltE) fromEscherichia coli

Peptidoglycan digestion by murein-degrading enzymes is a critical process in bacterial cell growth and/or cell division. The membrane-bound lytic murein transglycosylase A (MltA) is a murein-degrading enzyme; it catalyzes the cleavage of the β-1,4-glycosidic linkage between N-acetylmuramic acid and N-acetylglucosamine in peptidoglycans. Although substrate recognition and cleavage by MltA have been examined by previous structural and mutagenesis studies, the overall mechanism of MltA in conjunction with other functionally related molecules on the outer membrane of bacterial cells for peptidoglycan degradation has remained elusive. In this study, the crystal structure of MltA from the virulent human pathogen Acinetobacter baumannii is characterized and presented. The study indicated that MltA from A. baumannii forms homodimers via an extra domain which is specific to this species. Furthermore, the working mechanism of MltA with various functionally related proteins on the bacterial outer membrane was modeled based on the structural and biochemical analysis.

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Cryo-EM structure of the bacterial Ton motor subcomplex ExbB–ExbD provides information on structure and stoichiometry

Communications Biology ◽

10.1038/s42003-019-0604-2 ◽

2019 ◽

Vol 2 (1) ◽

Cited By ~ 16

Author(s):

Herve Celia ◽

Istvan Botos ◽

Xiaodan Ni ◽

Tara Fox ◽

Natalia De Val ◽

...

Keyword(s):

Crystal Structure ◽

Electron Microscopy ◽

High Resolution ◽

Outer Membrane ◽

Motor Function ◽

Structural Information ◽

Molecular Motor ◽

Single Copy ◽

Proton Motive Force ◽

Cryo Electron Microscopy

Abstract The TonB–ExbB–ExbD molecular motor harnesses the proton motive force across the bacterial inner membrane to couple energy to transporters at the outer membrane, facilitating uptake of essential nutrients such as iron and cobalamine. TonB physically interacts with the nutrient-loaded transporter to exert a force that opens an import pathway across the outer membrane. Until recently, no high-resolution structural information was available for this unique molecular motor. We published the first crystal structure of ExbB–ExbD in 2016 and showed that five copies of ExbB are arranged as a pentamer around a single copy of ExbD. However, our spectroscopic experiments clearly indicated that two copies of ExbD are present in the complex. To resolve this ambiguity, we used single-particle cryo-electron microscopy to show that the ExbB pentamer encloses a dimer of ExbD in its transmembrane pore, and not a monomer as previously reported. The revised stoichiometry has implications for motor function.

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High resolution STEM imaging study on high Tc superconductor YBa2CuaO7-x

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100106478 ◽

1988 ◽

Vol 46 ◽

pp. 882-883

Author(s):

H.-J. Ou ◽

J. M. Cowley

Keyword(s):

Crystal Structure ◽

High Resolution ◽

Grain Boundary ◽

Strong Field ◽

Imaging Study ◽

Structure Defects ◽

High Tc ◽

High Tc Superconductor ◽

Diffraction Patterns ◽

Lattice Planes

Using the dedicate VG-HB5 STEM microscope, the crystal structure of high Tc superconductor of YBa2Cu3O7-x has been studied via high resolution STEM (HRSTEM) imaging and nanobeam (∽3A) diffraction patterns. Figure 1(a) and 2(a) illustrate the HRSTEM image taken at 10' times magnification along [001] direction and [100] direction, respectively. In figure 1(a), a grain boundary with strong field contrast is seen between two crystal regions A and B. The grain boundary appears to be parallel to a (110) plane, although it is not possible to determine [100] and [001] axes as it is in other regions which contain twin planes [3]. Following the horizontal lattice lines, from left to right across the grain boundary, a lattice bending of ∽4° is noticed. Three extra lattice planes, indicated by arrows, were found to terminate at the grain boundary and form dislocations. It is believed that due to different chemical composition, such structure defects occur during crystal growth. No bending is observed along the vertical lattice lines.

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