4DCZ

Crystal structure of a domain from a mycoplasma genitalium terminal organelle protein

Summary for 4DCZ

• Entry DOI: 10.2210/pdb4dcz/pdb
• Descriptor: DnaJ-like protein MG200 (1 entity in total)
• Functional Keywords: dimer, intra-domain symmetry axis, unknown function
• Biological source: Mycoplasma genitalium
• Total number of polymer chains: 2
• Total formula weight: 21877.45

Authors

Calisto, B.M.,Martinelli, L.,Fita, I. (deposition date: 2012-01-18, release date: 2013-01-09, Last modification date: 2024-02-28)

Primary citation

Calisto, B.M.,Broto, A.,Martinelli, L.,Querol, E.,Pinol, J.,Fita, I.
The EAGR box structure: a motif involved in mycoplasma motility.
Mol.Microbiol., 86:382-393, 2012

PubMed Abstract: Mycoplasma 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 Enriched in Aromatic and Glycine Residues 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 MG200 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 MG200 variants lacking the EAGR box containing domain confirm the relevant and specific association of this domain with cell motility.

PubMed: 22925012
DOI: 10.1111/j.1365-2958.2012.08200.x

Experimental method

X-RAY DIFFRACTION (2.9 Å)