Gliding protein: Difference between revisions
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<StructureSection load='6izw' size=' | <StructureSection load='6izw' size='450' side='right' caption='Se-Met MglA (magenta) complex with MglB (green, pink), GTP-γS, Mg+2 ion (green) and sulfate (PDB code [[6izw]]).' scene='86/864720/Cv/1'> | ||
== Function == | == Function == | ||
'''Gliding protein''' or '''Mutual gliding-motility protein''' or '''Gliding motility protein''' (MglA and MglB). '''MglA''' is related to GTPase and is required for the normal operation of adventurous and social motility and multicellular development of some bacteria<ref>PMID:20196075</ref>. In''Myxococcus xanthus'' MglA regulates the movement of the bacteria on surfaces. '''MglB''' is MglA cognate GTPase activating protein<ref>PMID:31110363</ref>. | '''Gliding protein''' or '''Mutual gliding-motility protein''' or '''Gliding motility protein''' (MglA and MglB). '''MglA''' is related to GTPase and is required for the normal operation of adventurous and social motility and multicellular development of some bacteria<ref>PMID:20196075</ref>. In ''Myxococcus xanthus'' MglA regulates the movement of the bacteria on surfaces. '''MglB''' is MglA cognate GTPase activating protein<ref>PMID:31110363</ref>. | ||
== Structural highlights == | == Structural highlights == | ||
The 3D structure of the complex of MglA monomer and MglB dimer shows their hydrophilic and hydrophobic interacting surfaces<ref>PMID:31560685</ref>. | 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 <scene name='86/864720/Cv/6'>hydrophilic and hydrophobic interacting surfaces</scene><ref>PMID:31560685</ref>. <scene name='86/864720/Cv/9'>GTP-γS binding site</scene>. Water molecules are shown as red spheres. The bound <scene name='86/864720/Cv/10'>GTP-γS is hydrogen bonded to an Arg residue</scene> in MglA. <scene name='86/864720/Cv/12'>Mg coordination site</scene>. | ||
</StructureSection> | </StructureSection> | ||
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**[[3t12]] - TtMglA + MglB + GDP <br /> | **[[3t12]] - TtMglA + MglB + GDP <br /> | ||
**[[3t1q]] - TtMglA + MglB + GNP<br /> | **[[3t1q]] - TtMglA + MglB + GNP<br /> | ||
**[[6izw]] - MxMglA + MglB + GSP<br /> | **[[6izw]], [[6h5b]] - MxMglA + MglB + GSP<br /> | ||
*MglC | |||
**[[7ct3]], [[7cy1]] - MxMglC<br /> | |||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Latest revision as of 10:37, 4 August 2021
FunctionGliding protein or Mutual gliding-motility protein or Gliding motility protein (MglA and MglB). MglA is related to GTPase and is required for the normal operation of adventurous and social motility and multicellular development of some bacteria[1]. In Myxococcus xanthus MglA regulates the movement of the bacteria on surfaces. MglB is MglA cognate GTPase activating protein[2]. Structural highlightsThe 3D structure of the complex of and shows their [3]. . Water molecules are shown as red spheres. The bound in MglA. .
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3D structures of gliding protein3D structures of gliding protein
Updated on 04-August-2021
ReferencesReferences
- ↑ 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
- ↑ 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
- ↑ 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