Affinity Groups

There are no Affinity Groups associated with this topic. View All Affinity Groups.

Announcements

There are no announcements with this tag. View All Announcements.

Upcoming Events & Trainings

No events or trainings are currently scheduled.

Topics from Ask.CI

Loading topics from Ask.CI ...

Engagements

Prediction of Polymerization of the Yersinia Pestis Type III Secretion System
Nova Southeastern University

Yersinia pestis, the bacterium that causes the bubonic plague, uses a type III secretion system (T3SS) to inject toxins into host cells. The structure of the Y. pestis T3SS needle has not been modeled using AI or cryo-EM. T3SS in homologous bacteria have been solved using cryo-EM. Previously, we created possible hexamers of the Y. pestis T3SS needle protein, YscF, using CollabFold and AlphaFold2 Colab on Google Colab in an effort to understand more about the needle structure and calcium regulation of secretion. Hexamers and mutated hexamers were designed using data from a wet lab experiment by Torruellas et. al (2005). T3SS structures in homologous organisms show a 22 or 23mer structure where the rings of hexamers interlocked in layers. When folding was attempted with more than six monomers, we observed larger single rings of monomers. This revealed the inaccuracies of these online systems. To create a more accurate complete needle structure, a different computer software capable of creating a helical polymerized needle is required. The number of atoms in the predicted final needle is very high and more than our computational infrastructure can handle. For that reason, we need the computational resources of a supercomputer. We have hypothesized two ways to direct the folding that have the potential to result in a more accurate needle structure. The first option involves fusing the current hexamer structure into one protein chain, so that the software recognizes the hexamer as one protein. This will make it easier to connect multiple hexamers together. Alternatively, or additionally the cryo-EM structures of the T3SS of Shigella flexneri and Salmonella enterica Typhimurium can be used as models to guide the construction of the Y. pestis T3SS needle. The full AlphaFold library or a program like RoseTTAFold could help us predict protein-protein interactions more accurately for large structures. Based on our needs we have identified the TAMU ACES, Rockfish and Stampede-2 as promising resources for this project. The generated model of the Y. pestis T3SS YscF needle will provide insight into a possible structure of the needle. 

Status: Recruiting

People with Expertise

Chimdia Kabuo

Indiana University-Purdue University Fort Wayne

Programs

ACCESS CSSN

Roles

student-facilitator, cssn

Placeholder headshot

Expertise

+28 more tags

Alex Flosdorf

University of Rhode Island

Programs

CAREERS

Roles

student-facilitator

Expertise

Yating Fang

Rutgers University

Programs

Northeast

Roles

student-facilitator

Placeholder headshot

Expertise

People with Interest

Kyle Randall

Programs

ACCESS CSSN

Roles

student-facilitator

NASA Langley Picture

Interests

Paul Rulis

University of Missouri-Kansas City

Programs

Campus Champions

Roles

researcher/educator, research computing facilitator

Paul Rulis

Interests

Doruk Alp MUTLU

Michigan State University

Programs

ACCESS CSSN

Roles

student-facilitator

profile photo

Interests