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Crystal structures of the helix-loop-helix calcium-binding proteins.
Insights into the respiratory electron transfer pathway from the structure of nitrate reductase A
The NarGHI structure identifies the number, coordination scheme and environment of the redox-active prosthetic groups, a unique coordination of the molybdenum atom, the first structural evidence for the role of an open bicyclic form of themolybdo-bis in the catalytic mechanism and a novel fold of the membrane anchor subunit.
Structural analysis of the essential self-cleaving type III secretion proteins EscU and SpaS
It is shown that a surface type II β-turn in the Escherichia coli protein EscU undergoes auto-cleavage by a mechanism involving cyclization of a strictly conserved asparagine residue in order to promote a secretion-competent state.
Assembly, structure, function and regulation of type III secretion systems
Current knowledge of the structure and function of T3SSs is summarized, which should aid mechanism-based drug design and facilitate their manipulation for biotechnological applications.
A conserved structural motif mediates formation of the periplasmic rings in the type III secretion system
Using an integrated structural and experimental approach, ring models for the periplasmic domain of EscC are generated and placed in the context of the assembled T3SS, providing evidence for direct interaction between the outer membrane and inner membrane ring components and an unprecedented span of the outer membranes secretin.
Structural characterization of the molecular platform for type III secretion system assembly
Crystal packing analysis and molecular modelling indicate that EscJ could form a large 24-subunit ‘ring’ superstructure with extensive grooves, ridges and electrostatic features, and it is proposed that the YscJ/PrgK protein family functions as an essential molecular platform for TTSS assembly.
Enteropathogenic Escherichia coli translocated intimin receptor, Tir, requires a specific chaperone for stable secretion
Results indicate that CesT is a Tir chaperone that may act as an anti‐degradation factor by specifically binding to its amino‐terminus, forming a multimeric stabilized complex.
Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution
The X-ray crystal structure of the molecular complex of penicillin G with a deacylation-defective mutant of the RTEM-1 β-lactamase from Escherichia coli shows how these antibiotics are recognized and…
Studies of a Ring-Cleaving Dioxygenase Illuminate the Role of Cholesterol Metabolism in the Pathogenesis of Mycobacterium tuberculosis
While cholesterol metabolism by M. tuberculosis appears to be most important during the chronic stage of infection, it begins much earlier and may contribute to the pathogen's dissemination within the host, providing insights into the binding of catechols by extradiol dioxygenases and facilitate inhibitor design.
Structural analysis of a prototypical ATPase from the type III secretion system
- R. Zarivach, M. Vučković, W. Deng, B. Finlay, N. Strynadka
- BiologyNature Structural &Molecular Biology
- 21 January 2007
The 1.8-Å-resolution crystal structure of the catalytic domain of the prototypical T3SS ATPase EscN from enteropathogenic Escherichia coli is presented and it is shown that T3 SS ATPase activity is dependent on EscN oligomerization and the molecular features and possible functional implications of a hexameric ring model are described.