G. Waksman

Publications369
h-index78
Citations21,239
Highly Influential Citations1,078
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Structure of a Type IV Secretion System Core Complex
TLDR
Overall, the T4SS core complex structure is different in both architecture and composition from the other known double membrane–spanning secretion system that has been structurally characterized.
Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide incorporation
TLDR
These structures provide the first direct evidence in DNA polymerase I enzymes of a large conformational change responsible for assembling an active ternary complex.
Secretion systems in Gram-negative bacteria: structural and mechanistic insights
TLDR
The structural and mechanistic relationships between these single- and double-membrane-embedded systems are explored, and how this knowledge can be exploited for the development of new antimicrobial strategies are discussed.
Structure of the outer membrane complex of a type IV secretion system
TLDR
This structure establishes VirB10 as the only known protein crossing both membranes of Gram-negative bacteria, and the largest determined for an outer-membrane channel and is unprecedented in being composed of three proteins.
The structural biology of type IV secretion systems
TLDR
This Review focuses on the structural advances that have been made over the past 10 years and how the corresponding structural insights have helped to elucidate many of the details of the mechanism of type IV secretion.
Major Domain Swiveling Revealed by the Crystal Structures of Complexes of E. coli Rep Helicase Bound to Single-Stranded DNA and ADP
Synthetic protein transduction domains: enhanced transduction potential in vitro and in vivo.
TLDR
It is reported here that the modeled structure of the TAT PTD is a strong amphipathic helix and a series of synthetic PTDs are synthesized that strengthen the alpha-helical content and optimize the placement of arginine residues.
Structural basis of chaperone function and pilus biogenesis.
TLDR
The structure of the PapD-PapK chaperone-subunit complex suggests that during pilus biogenesis, every subunit completes the immunoglobulin-like fold of its neighboring subunit via a mechanism termed donor strand exchange.
The biology and enzymology of protein N-myristoylation.
Chaperone Priming of Pilus Subunits Facilitates a Topological Transition that Drives Fiber Formation
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