Hongjin Zheng

Structural studies of a bacterial siderophore ABC importer YbtPQ

Lead Institution

University of Colorado Anschutz Medical Campus

Principal Investigator

Hongjin Zheng

Iron (Fe) is an essential element for not only the well-being of hosts, but also the growth and virulence of microbes(Begg, 2019). One of the major Fe uptake processes in bacteria is through…

The structure of Streptococcus pneumoniae IgA1 Protease in complex with its IgA1 substrate.

Lead Institution

University of Colorado at Denver

Principal Investigator

Elan Eisenmesser

We propose completing the first complex of a bacterial IgA1 Protease (IgA1P) in complex with its human IgA1 substrate. Many opportunistic bacteria produce an IgA1P to cleave their human host IgA1…

Towards Better Understanding of the Siderophore Uptake Process in Escherichia coli

Lead Institution

University of Colorado Anschutz Medical Campus

Principal Investigator

Hongjin Zheng

Using siderophores to scavenge metal ions from the host is critical to the thrive of the bacteria during infections. The metal-chelated siderophores are reimported into the bacterial cells through a…

Collaborative Access Team: Pacific Northwest Cryo-EM Center (PNCC)

Lead Institution

Environmental Molecular Sciences Laboratory

Principal Investigator

James Evans

PNNL will create and operate the Pacific Northwest Center for Cryo-EM (PNCC), a state-of-the-art national center for cryo-electron microscopy (Cryo-EM) that will rapidly and efficiently collect and…

TheThe Streptococcus pneumoniae IgA1 Protease: from molecular mechanism to vaccine development.

Lead Institution

University of Colorado at Denver

Principal Investigator

Elan Eisenmesser

Streptococcus pneumoniae remains a “major global public health problem” according to the World Health Organization with an alarming increase in non-vaccine serotypes, prompting the immediate need to…

EMSL Science Overview

Hongjin Zheng

Projects

Structural studies of a bacterial siderophore ABC importer YbtPQ

The structure of Streptococcus pneumoniae IgA1 Protease in complex with its IgA1 substrate.

Towards Better Understanding of the Siderophore Uptake Process in Escherichia coli

Collaborative Access Team: Pacific Northwest Cryo-EM Center (PNCC)

TheThe Streptococcus pneumoniae IgA1 Protease: from molecular mechanism to vaccine development.