Crystal structure of the usher chaperone YadV reveals a monomer with the proline lock in closed conformation suggestive of an intermediate state

AbstractCell surface pili assembled by the chaperone ‐usher (CU) pathway play a crucial role in the adhesion of uropathogenicEscherichia coli. YadV is the chaperone component of the CU pathway of Yad pili. Here, we report the crystal structure of YadV fromE. coli. In contrast to major usher chaperones, YadV is a monomer in solution as well as in the crystallographic symmetry, and the monomeric form is a preferred state for interacting with pilus subunits. Moreover, we observed a closed conformation for the proline lock, a crucial structural element for chaperone –pilus subunit interaction. MD simulation shows that the closed state of the proline lock is not energetically stable. Thus, the structure of monomeric YadV with its closed proline lock may serve as an intermediate state to provide suitable access to pilus subunits.

Source: FEBS Letters - July 9, 2020 Category: Biochemistry Authors: Nishant Kumar Pandey, Garima Verma, Gajraj Singh Kushwaha, Mrutyunjay Suar, Neel Sarovar Bhavesh Tags: RESEARCH LETTER Source Type: research