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Crystal structure of the usher chaperone YadV reveals a monomer with the proline lock in closed conformation suggestive of an intermediate state
Author(s) -
Pandey Nishant Kumar,
Verma Garima,
Kushwaha Gajraj Singh,
Suar Mrutyunjay,
Bhavesh Neel Sarovar
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13883
Subject(s) - pilus , chaperone (clinical) , monomer , crystallography , protein subunit , proline , crystal structure , chemistry , protein folding , biophysics , escherichia coli , stereochemistry , biochemistry , biology , amino acid , polymer , medicine , organic chemistry , pathology , gene
Cell surface pili assembled by the chaperone–usher (CU) pathway play a crucial role in the adhesion of uropathogenic Escherichia coli . YadV is the chaperone component of the CU pathway of Yad pili. Here, we report the crystal structure of YadV from E. 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.