5YMX

Myxococcus xanthus MglA in GDP bound conformation

Summary for 5YMX

• Entry DOI: 10.2210/pdb5ymx/pdb
• Descriptor: Mutual gliding-motility protein MglA, GUANOSINE-5'-DIPHOSPHATE, IMIDAZOLE, ... (6 entities in total)
• Functional Keywords: small ras-like gtpase, cytosolic, myxococcus motility protein, spatial oscillation, signaling protein, hydrolase
• Biological source: Myxococcus xanthus (strain DK 1622)
• Total number of polymer chains: 2
• Total formula weight: 47297.66

Authors

Baranwal, J.,Gayathri, P. (deposition date: 2017-10-22, release date: 2018-10-24, Last modification date: 2023-11-22)

Primary citation

Baranwal, J.,Lhospice, S.,Kanade, M.,Chakraborty, S.,Gade, P.R.,Harne, S.,Herrou, J.,Mignot, T.,Gayathri, P.
Allosteric regulation of a prokaryotic small Ras-like GTPase contributes to cell polarity oscillations in bacterial motility.
Plos Biol., 17:e3000459-e3000459, 2019

PubMed Abstract: Mutual gliding motility A (MglA), a small Ras-like GTPase; Mutual gliding motility B (MglB), its GTPase activating protein (GAP); and Required for Motility Response Regulator (RomR), a protein that contains a response regulator receiver domain, are major components of a GTPase-dependent biochemical oscillator that drives cell polarity reversals in the bacterium Myxococcus xanthus. We report the crystal structure of a complex of M. xanthus MglA and MglB, which reveals that the C-terminal helix (Ct-helix) from one protomer of the dimeric MglB binds to a pocket distal to the active site of MglA. MglB increases the GTPase activity of MglA by reorientation of key catalytic residues of MglA (a GAP function) combined with allosteric regulation of nucleotide exchange by the Ct-helix (a guanine nucleotide exchange factor [GEF] function). The dual GAP-GEF activities of MglB accelerate the rate of GTP hydrolysis over multiple enzymatic cycles. Consistent with its GAP and GEF activities, MglB interacts with MglA bound to either GTP or GDP. The regulation is essential for cell polarity, because deletion of the Ct-helix causes bipolar localization of MglA, MglB, and RomR, thereby causing reversal defects in M. xanthus. A bioinformatics analysis reveals the presence of Ct-helix in homologues of MglB in other bacterial phyla, suggestive of the prevalence of the allosteric mechanism among other prokaryotic small Ras-like GTPases.

PubMed: 31560685
DOI: 10.1371/journal.pbio.3000459

Experimental method

X-RAY DIFFRACTION (1.35 Å)