3T1T
MglA bound to GDP in P1 tetrameric arrangement
Summary for 3T1T
Entry DOI | 10.2210/pdb3t1t/pdb |
Related | 3T12 3T1O 3T1Q 3T1R 3T1S 3T1V 3T1X |
Descriptor | Gliding protein mglA, GUANOSINE-5'-DIPHOSPHATE (3 entities in total) |
Functional Keywords | g domain containg protein, bacterial gtpase, bacterial polarity, motility, alpha/beta protein, hydrolase |
Biological source | Thermus thermophilus |
Total number of polymer chains | 4 |
Total formula weight | 90707.93 |
Authors | Miertzschke, M.,Vetter, I.R.,Koerner, C.,Wittinghofer, A. (deposition date: 2011-07-22, release date: 2011-08-31, Last modification date: 2024-11-06) |
Primary citation | Miertzschke, M.,Koerner, C.,Vetter, I.R.,Keilberg, D.,Hot, E.,Leonardy, S.,Sogaard-Andersen, L.,Wittinghofer, A. Structural analysis of the Ras-like G protein MglA and its cognate GAP MglB and implications for bacterial polarity. Embo J., 30:4185-4197, 2011 Cited by PubMed Abstract: The bacterium Myxococcus xanthus uses a G protein cycle to dynamically regulate the leading/lagging pole polarity axis. The G protein MglA is regulated by its GTPase-activating protein (GAP) MglB, thus resembling Ras family proteins. Here, we show structurally and biochemically that MglA undergoes a dramatic, GDP-GTP-dependent conformational change involving a screw-type forward movement of the central β2-strand, never observed in any other G protein. This movement and complex formation with MglB repositions the conserved residues Arg53 and Gln82 into the active site. Residues required for catalysis are thus not provided by the GAP MglB, but by MglA itself. MglB is a Roadblock/LC7 protein and functions as a dimer to stimulate GTP hydrolysis in a 2:1 complex with MglA. In vivo analyses demonstrate that hydrolysis mutants abrogate Myxococcus' ability to regulate its polarity axis changing the reversal behaviour from stochastic to oscillatory and that both MglA GTPase activity and MglB GAP catalysis are essential for maintaining a proper polarity axis. PubMed: 21847100DOI: 10.1038/emboj.2011.291 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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