Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2023 Sep 28;14:1268820. doi: 10.3389/fmicb.2023.1268820

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

Copyright © 2023 Akritidou and Thurtle-Schmidt.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

PMC Copyright notice

Structural similarity and multimeric assembly of Class 1 and Class 2 OLD proteins. (A) Schematics showing domain organization within Class 1 T. scotoductus OLD and Class 2 B. cereus GajA OLD proteins. A dimerization domain (tan) is inserted into each ABC ATPase domain (blue). The larger size of BcGajA arises from a helical insert into the Toprim domain (red) that is conserved among Class 2 OLD proteins and makes them larger than Class 1 OLD proteins by about 50 amino acids on average. (B) Structural superposition of TsOLD (PDB: 6P74) and BcGajA (PDB: 8SM3) full-length monomers shows structural similarity (RMSD = 4.4 Å) despite only 22.2% sequence identity. (C) TsOLD dimerizes and BcGajA tetramerizes in crystal structures, but in neither structure are the ATPases poised for ATP hydrolysis. (D) Two separate GajB dimers (green) bind to a GajA homotetramer to assemble an octameric GajAB complex.