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The EAGR box structure: a motif involved in mycoplasma motility
Author(s) -
Calisto Bárbara M.,
Broto Alícia,
Martinelli Luca,
Querol Enrique,
Piñol Jaume,
Fita Ignacio
Publication year - 2012
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2012.08200.x
Subject(s) - biology , organelle , protein subunit , mycoplasma genitalium , microbiology and biotechnology , virulence , dimer , protein domain , motility , genetics , gene , physics , nuclear magnetic resonance , chlamydia trachomatis , immunology
Summary M ycoplasma genitalium is an emerging human pathogen with the smallest genome found among self‐replicating organisms. M . genitalium presents a complex cytoskeleton with a differentiated protrusion known as the terminal organelle. This polar structure plays a central role in functions essential for the virulence of the microorganism, such as motility and cell‐host adhesion. A well‐conserved E nriched in A romatic and G lycine R esidues motif, the EAGR box, is present in many of the proteins found in the terminal organelle. We determined the crystal structure of the globular domain from M . genitalium MG 200 that contains an EAGR box. This structural information is the first at near atomic resolution for the components of the terminal organelle. The structure revealed a dimer stabilized by a compact hydrophobic core that extends throughout the dimer interface. Monomers present a new fold that contains an accurate intra‐subunit symmetry relating two conspicuous hairpins. Some features, such as the domain plasticity and the presence and organization of the intra‐ and inter‐subunit symmetry axes, support a role for the EAGR box in protein–protein interactions. Genetic, biochemical and microcinematography analyses of MG 200 variants lacking the EAGR box containing domain confirm the relevant and specific association of this domain with cell motility.