1RLU
Mycobacterium tuberculosis FtsZ in complex with GTP-gamma-S
Summary for 1RLU
Entry DOI | 10.2210/pdb1rlu/pdb |
Related | 1RQ2 1RQ7 |
Descriptor | Cell division protein ftsZ, 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE, GLYCEROL, ... (4 entities in total) |
Functional Keywords | cell cycle, tubulin, gtpase, signaling protein |
Biological source | Mycobacterium tuberculosis |
Total number of polymer chains | 2 |
Total formula weight | 78777.35 |
Authors | Leung, A.K.W.,White, E.L.,Ross, L.J.,Reynolds, R.C.,DeVito, J.A.,Borhani, D.W. (deposition date: 2003-11-26, release date: 2004-08-31, Last modification date: 2023-08-23) |
Primary citation | Leung, A.K.,Lucile White, E.,Ross, L.J.,Reynolds, R.C.,DeVito, J.A.,Borhani, D.W. Structure of Mycobacterium tuberculosis FtsZ reveals unexpected, G protein-like conformational switches. J.Mol.Biol., 342:953-970, 2004 Cited by PubMed Abstract: We report three crystal structures of the Mycobacterium tuberculosis cell division protein FtsZ, as the citrate, GDP, and GTPgammaS complexes, determined at 1.89, 2.60, and 2.08A resolution. MtbFtsZ crystallized as a tight, laterally oriented dimer distinct from the longitudinal polymer observed for alphabeta-tubulin. Mutational data on Escherichia coli FtsZ suggest that this dimer interface is important for proper protofilament and "Z-ring" assembly and function. An alpha-to-beta secondary structure conformational switch at the dimer interface is spatially analogous to, and has many of the hallmarks of, the Switch I conformational changes exhibited by G-proteins upon activation. The presence of a gamma-phosphate in the FtsZ active site modulates the conformation of the "tubulin" loop T3 (spatially analogous to the G-protein Switch II); T3 switching upon gamma-phosphate ligation is directly coupled to the alpha-to-beta switch by steric overlap. The dual conformational switches observed here for the first time in an FtsZ link GTP binding and hydrolysis to FtsZ (and tubulin) lateral assembly and Z-ring contraction, and they are suggestive of an underappreciated functional analogy between FtsZ, tubulin and G-proteins. PubMed: 15342249DOI: 10.1016/j.jmb.2004.07.061 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.08 Å) |
Structure validation
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