5ghu | pdb_00005ghu

Crystal structure of YadV chaperone at 1.63 Angstrom

spinqualitylabelsall models 5ghu, resolution 1.63Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5ghu is a 1 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, CL, FMT, PGE Gene: ecpD (ECOLI) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [YADV_ECOLI] Part of the yadCKLM-htrE-yadVN fimbrial operon. Could contribute to adhesion to various surfaces in specific environmental niches. Publication Abstract from PubMed 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. Crystal structure of the usher chaperone YadV reveals a monomer with the proline lock in closed conformation suggestive of an intermediate state.,Pandey NK, Verma G, Kushwaha GS, Suar M, Bhavesh NS FEBS Lett. 2020 Jul 10. doi: 10.1002/1873-3468.13883. PMID:32649775 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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