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Gliding protein

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== Structural highlights ==
== Structural highlights ==
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The 3D structure of the complex of MglA monomer and MglB dimer shows their hydrophilic and hydrophobic interacting surfaces<ref>PMID:31560685</ref>. The bound GTP-γS is hydrogen bonded to an Arg residue in MglA.
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The 3D structure of the complex of <scene name='86/864720/Cv/2'>MglA monomer</scene> and <scene name='86/864720/Cv/3'>MglB dimer</scene> shows their hydrophilic and hydrophobic interacting surfaces<ref>PMID:31560685</ref>. The bound GTP-γS is hydrogen bonded to an Arg residue in MglA.
</StructureSection>
</StructureSection>

Revision as of 14:15, 20 October 2020

Se-Met MglA (magenta) complex with MglB (green, pink), GTP-γS, Mg+2 ion (green) and sulfate (PDB code 6izw).

Drag the structure with the mouse to rotate

3D structures of gliding protein

Updated on 20-October-2020

References

  1. ↑ Patryn J, Allen K, Dziewanowska K, Otto R, Hartzell PL. Localization of MglA, an essential gliding motility protein in Myxococcus xanthus. Cytoskeleton (Hoboken). 2010 May;67(5):322-37. doi: 10.1002/cm.20447. PMID:20196075 doi:http://dx.doi.org/10.1002/cm.20447
  2. ↑ Szadkowski D, Harms A, Carreira LAM, Wigbers M, Potapova A, Wuichet K, Keilberg D, Gerland U, Sogaard-Andersen L. Spatial control of the GTPase MglA by localized RomR-RomX GEF and MglB GAP activities enables Myxococcus xanthus motility. Nat Microbiol. 2019 Aug;4(8):1344-1355. doi: 10.1038/s41564-019-0451-4. Epub 2019, May 20. PMID:31110363 doi:http://dx.doi.org/10.1038/s41564-019-0451-4
  3. ↑ Baranwal J, Lhospice S, Kanade M, Chakraborty S, Gade PR, 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. 2019 Sep 27;17(9):e3000459. doi: 10.1371/journal.pbio.3000459., eCollection 2019 Sep. PMID:31560685 doi:http://dx.doi.org/10.1371/journal.pbio.3000459

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Michal Harel, Alexander Berchansky

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