5IRR

Crystal structure of Septin GTPase domain from Chlamydomonas reinhardtii

Summary for 5IRR

• Entry DOI: 10.2210/pdb5irr/pdb
• Descriptor: Septin-like protein, MAGNESIUM ION, 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE, ... (4 entities in total)
• Functional Keywords: septin, gtpase domain, hydrolase
• Biological source: Chlamydomonas reinhardtii
• Total number of polymer chains: 2
• Total formula weight: 73251.81

Authors

Pinto, A.P.A.,Pereira, H.M.,Navarro, M.V.A.S.,Brandao-Neto, J.,Garratt, R.C.,Araujo, A.P.U. (deposition date: 2016-03-14, release date: 2017-04-26, Last modification date: 2024-10-16)

Primary citation

Pinto, A.P.A.,Pereira, H.M.,Zeraik, A.E.,Ciol, H.,Ferreira, F.M.,Brandao-Neto, J.,DeMarco, R.,Navarro, M.V.A.S.,Risi, C.,Galkin, V.E.,Garratt, R.C.,Araujo, A.P.U.
Filaments and fingers: Novel structural aspects of the single septin from Chlamydomonas reinhardtii.
J. Biol. Chem., 292:10899-10911, 2017

PubMed Abstract: Septins are filament-forming GTP-binding proteins involved in many essential cellular events related to cytoskeletal dynamics and maintenance. Septins can self-assemble into heterocomplexes, which polymerize into highly organized, cell membrane-interacting filaments. The number of septin genes varies among organisms, and although their structure and function have been thoroughly studied in opisthokonts (including animals and fungi), no structural studies have been reported for other organisms. This makes the single septin from (CrSEPT) a particularly attractive model for investigating whether functional homopolymeric septin filaments also exist. CrSEPT was detected at the base of the flagella in , suggesting that CrSEPT is involved in the formation of a membrane-diffusion barrier. Using transmission electron microscopy, we observed that recombinant CrSEPT forms long filaments with dimensions comparable with those of the canonical structure described for opisthokonts. The GTP-binding domain of CrSEPT purified as a nucleotide-free monomer that hydrolyzes GTP and readily binds its analog guanosine 5'-3--(thio)triphosphate. We also found that upon nucleotide binding, CrSEPT formed dimers that were stabilized by an interface involving the ligand (G-interface). Across this interface, one monomer supplied a catalytic arginine to the opposing subunit, greatly accelerating the rate of GTP hydrolysis. This is the first report of an arginine finger observed in a septin and suggests that CrSEPT may act as its own GTP-activating protein. The finger is conserved in all algal septin sequences, suggesting a possible correlation between the ability to form homopolymeric filaments and the accelerated rate of hydrolysis that it provides.

PubMed: 28476887
DOI: 10.1074/jbc.M116.762229

Experimental method

X-RAY DIFFRACTION (2.04 Å)