# Unraveling the mechanism by which the BAM complex mediates OMP biogenesis

> **NIH NIH R01** · PURDUE UNIVERSITY · 2020 · $300,852

## Abstract

Project Summary
Gram-negative bacteria, such as E. coli, have an outer membrane which provides nutrients and added
protection for the cell. The outer membrane also contains proteins that can enable pathogenic bacteria to
evade host immune responses and cause a number of serious infectious diseases. Despite the
importance of these outer membrane proteins (OMPs) for cell survival and virulence, little is known about
how these proteins are folded and inserted into the outer membrane. However, in E. coli, we know that a
200 kDa five-component complex called the β-barrel assembly machinery (BAM) complex mediates the
biogenesis of these membrane proteins. In the last decade, the individual structures of components of the
BAM complex have been reported with the structure of BamA, the central component, providing the most
useful clues to how the BAM complex may function. Here, it was revealed that BamA may destabilize the
local membrane, thereby promoting protein folding and insertion into the membrane. Recently, our work
and others’ have determined the structure of the BAM complex, revealing unprecedented conformational
changes within the barrel domain of BamA. Our work here will utilize these structures to study the role of
the conformational changes for the function of the BAM complex in OMP biogenesis. Additionally, we will
determine how substrate OMPs are recognized by the BAM complex and how they interact with BAM
during folding into the membrane. Lastly, we will use structural biology methods to study the BAM complex
in a lipid bilayer and in the presence of substrates. Our proposed studies will provide crucial functional and
structural insight towards unraveling how the BAM complex performs its essential role in bacteria.

## Key facts

- **NIH application ID:** 9974536
- **Project number:** 5R01GM127884-02
- **Recipient organization:** PURDUE UNIVERSITY
- **Principal Investigator:** Nicholas Noinaj
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2020
- **Award amount:** $300,852
- **Award type:** 5
- **Project period:** 2019-07-08 → 2023-05-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/9974536

## Citation

> US National Institutes of Health, RePORTER application 9974536, Unraveling the mechanism by which the BAM complex mediates OMP biogenesis (5R01GM127884-02). Retrieved via AI Analytics 2026-05-22 from https://api.ai-analytics.org/grant/nih/9974536. Licensed CC0.

---

*[NIH grants dataset](/datasets/nih-grants) · CC0 1.0*