5HTL

Structure of MshE with cdg

Summary for 5HTL

• Entry DOI: 10.2210/pdb5htl/pdb
• Descriptor: MSHA biogenesis protein MshE, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) (3 entities in total)
• Functional Keywords: mshe, c-di-gmp, biosynthetic protein
• Biological source: Vibrio cholerae
• Total number of polymer chains: 2
• Total formula weight: 33963.53

Authors

Chin, K.H.,Wang, Y.C. (deposition date: 2016-01-27, release date: 2016-10-05, Last modification date: 2024-10-09)

Primary citation

Wang, Y.C.,Chin, K.H.,Tu, Z.L.,He, J.,Jones, C.J.,Sanchez, D.Z.,Yildiz, F.H.,Galperin, M.Y.,Chou, S.H.
Nucleotide binding by the widespread high-affinity cyclic di-GMP receptor MshEN domain.
Nat Commun, 7:12481-12481, 2016

PubMed Abstract: C-di-GMP is a bacterial second messenger regulating various cellular functions. Many bacteria contain c-di-GMP-metabolizing enzymes but lack known c-di-GMP receptors. Recently, two MshE-type ATPases associated with bacterial type II secretion system and type IV pilus formation were shown to specifically bind c-di-GMP. Here we report crystal structure of the MshE N-terminal domain (MshEN1-145) from Vibrio cholerae in complex with c-di-GMP at a 1.37 Å resolution. This structure reveals a unique c-di-GMP-binding mode, featuring a tandem array of two highly conserved binding motifs, each comprising a 24-residue sequence RLGxx(L/V/I)(L/V/I)xxG(L/V/I)(L/V/I)xxxxLxxxLxxQ that binds half of the c-di-GMP molecule, primarily through hydrophobic interactions. Mutating these highly conserved residues markedly reduces c-di-GMP binding and biofilm formation by V. cholerae. This c-di-GMP-binding motif is present in diverse bacterial proteins exhibiting binding affinities ranging from 0.5 μM to as low as 14 nM. The MshEN domain contains the longest nucleotide-binding motif reported to date.

PubMed: 27578558
DOI: 10.1038/ncomms12481

Experimental method

X-RAY DIFFRACTION (1.371 Å)