2NB9

Solution structure of ZitP zinc finger

Summary for 2NB9

• Entry DOI: 10.2210/pdb2nb9/pdb
• NMR Information: BMRB: 25967
• Descriptor: Uncharacterized protein, ZINC ION (2 entities in total)
• Functional Keywords: zinc finger, unknown function
• Biological source: Caulobacter crescentus
• Total number of polymer chains: 1
• Total formula weight: 5564.70

Authors

Campagne, S.,Berge, M.,Viollier, P.H.,Allain, F.H.-T. (deposition date: 2016-02-01, release date: 2016-12-14, Last modification date: 2024-05-15)

Primary citation

Berge, M.,Campagne, S.,Mignolet, J.,Holden, S.,Theraulaz, L.,Manley, S.,Allain, F.H.,Viollier, P.H.
Modularity and determinants of a (bi-)polarization control system from free-living and obligate intracellular bacteria.
Elife, 5:-, 2016

PubMed Abstract: Although free-living and obligate intracellular bacteria are both polarized it is unclear whether the underlying polarization mechanisms and effector proteins are conserved. Here we dissect at the cytological, functional and structural level a conserved polarization module from the free living α-proteobacterium and an orthologous system from an obligate intracellular (rickettsial) pathogen. The NMR solution structure of the zinc-finger (ZnR) domain from the bifunctional and bipolar ZitP pilus assembly/motility regulator revealed conserved interaction determinants for PopZ, a bipolar matrix protein that anchors the ParB centromere-binding protein and other regulatory factors at the poles. We show that ZitP regulates cytokinesis and the localization of ParB and PopZ, targeting PopZ independently of the previously known binding sites for its client proteins. Through heterologous localization assays with rickettsial ZitP and PopZ orthologs, we document the shared ancestries, activities and structural determinants of a (bi-)polarization system encoded in free-living and obligate intracellular α-proteobacteria.

PubMed: 28008852
DOI: 10.7554/eLife.20640

Experimental method

SOLUTION NMR