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1RLU

Mycobacterium tuberculosis FtsZ in complex with GTP-gamma-S

Summary for 1RLU
Entry DOI10.2210/pdb1rlu/pdb
Related1RQ2 1RQ7
DescriptorCell division protein ftsZ, 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE, GLYCEROL, ... (4 entities in total)
Functional Keywordscell cycle, tubulin, gtpase, signaling protein
Biological sourceMycobacterium tuberculosis
Total number of polymer chains2
Total formula weight78777.35
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 citationLeung, 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: 15342249
DOI: 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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数据于2024-10-30公开中

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