5HSZ

Structure of the K. pneumonia SlmA protein bound to the C-terminal tail of the cytoskeletal cell division protein FtsZ

Summary for 5HSZ

• Entry DOI: 10.2210/pdb5hsz/pdb
• Descriptor: Nucleoid occlusion factor SlmA, C-terminal Tail of FtsZ, SULFATE ION, ... (4 entities in total)
• Functional Keywords: slma, nucleoid occlusion, ftsz, z-ring, cell division, cytokinesis, cell cycle
• Biological source: Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578); More
• Cellular location: Cytoplasm, nucleoid : A6TFN2
• Total number of polymer chains: 3
• Total formula weight: 46869.99

Authors

Zeng, W.,Schumacher, M.A. (deposition date: 2016-01-26, release date: 2016-04-13, Last modification date: 2024-03-06)

Primary citation

Schumacher, M.A.,Zeng, W.
Structures of the nucleoid occlusion protein SlmA bound to DNA and the C-terminal domain of the cytoskeletal protein FtsZ.
Proc.Natl.Acad.Sci.USA, 113:4988-4993, 2016

PubMed Abstract: Cell division in most prokaryotes is mediated by FtsZ, which polymerizes to create the cytokinetic Z ring. Multiple FtsZ-binding proteins regulate FtsZ polymerization to ensure the proper spatiotemporal formation of the Z ring at the division site. The DNA-binding protein SlmA binds to FtsZ and prevents Z-ring formation through the nucleoid in a process called "nucleoid occlusion" (NO). As do most FtsZ-accessory proteins, SlmA interacts with the conserved C-terminal domain (CTD) that is connected to the FtsZ core by a long, flexible linker. However, SlmA is distinct from other regulatory factors in that it must be DNA-bound to interact with the FtsZ CTD. Few structures of FtsZ regulator-CTD complexes are available, but all reveal the CTD bound as a helix. To deduce the molecular basis for the unique SlmA-DNA-FtsZ CTD regulatory interaction and provide insight into FtsZ-regulator protein complex formation, we determined structures of Escherichia coli, Vibrio cholera, and Klebsiella pneumonia SlmA-DNA-FtsZ CTD ternary complexes. Strikingly, the FtsZ CTD does not interact with SlmA as a helix but binds as an extended conformation in a narrow, surface-exposed pocket formed only in the DNA-bound state of SlmA and located at the junction between the DNA-binding and C-terminal dimer domains. Binding studies are consistent with the structure and underscore key interactions in complex formation. Combined, these data reveal the molecular basis for the SlmA-DNA-FtsZ interaction with implications for SlmA's NO function and underscore the ability of the FtsZ CTD to adopt a wide range of conformations, explaining its ability to bind diverse regulatory proteins.

PubMed: 27091999
DOI: 10.1073/pnas.1602327113

Experimental method

X-RAY DIFFRACTION (2.3 Å)