6hjh: Difference between revisions

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'''Unreleased structure'''


The entry 6hjh is ON HOLD until Paper Publication
==Myxococcus xanthus MglA bound to GDP==
<StructureSection load='6hjh' size='340' side='right'caption='[[6hjh]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hjh]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HJH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HJH FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6hjh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hjh OCA], [http://pdbe.org/6hjh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hjh RCSB], [http://www.ebi.ac.uk/pdbsum/6hjh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hjh ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/MGLA_MYXXD MGLA_MYXXD]] Required for multicellular development and for both mechanisms of gliding: social (S) and adventurous (A) motility. Acts as an intracellular switch to coordinate A and S motilities. Controls the direction of gliding and gliding speed.<ref>PMID:10198026</ref> <ref>PMID:1938957</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In Myxococcus xanthus, directed movement is controlled by pole-to-pole oscillations of the small GTPase MglA and its GAP MglB. Direction reversals require that MglA is inactivated by MglB, yet paradoxically MglA and MglB are located at opposite poles at reversal initiation. Here we report the complete MglA/MglB structural cycle combined to GAP kinetics and in vivo motility assays, which uncovers that MglA is a three-state GTPase and suggests a molecular mechanism for concerted MglA/MglB relocalizations. We show that MglA has an atypical GTP-bound state (MglA-GTP*) that is refractory to MglB and is re-sensitized by a feedback mechanism operated by MglA-GDP. By identifying and mutating the pole-binding region of MglB, we then provide evidence that the MglA-GTP* state exists in vivo. These data support a model in which MglA-GDP acts as a soluble messenger to convert polar MglA-GTP* into a diffusible MglA-GTP species that re-localizes to the opposite pole during reversals.


Authors: Varela, P.F., Cherfils, J.
MglA functions as a three-state GTPase to control movement reversals of Myxococcus xanthus.,Galicia C, Lhospice S, Varela PF, Trapani S, Zhang W, Navaza J, Herrou J, Mignot T, Cherfils J Nat Commun. 2019 Nov 22;10(1):5300. doi: 10.1038/s41467-019-13274-3. PMID:31757955<ref>PMID:31757955</ref>


Description: Myxococcus xanthus MglA bound to GDP
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6hjh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Cherfils, J]]
[[Category: Cherfils, J]]
[[Category: Varela, P.F]]
[[Category: Varela, P F]]
[[Category: Cytosolic protein]]
[[Category: Small gtpase]]

Latest revision as of 10:56, 4 December 2019

Myxococcus xanthus MglA bound to GDPMyxococcus xanthus MglA bound to GDP

Structural highlights

6hjh is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MGLA_MYXXD] Required for multicellular development and for both mechanisms of gliding: social (S) and adventurous (A) motility. Acts as an intracellular switch to coordinate A and S motilities. Controls the direction of gliding and gliding speed.[1] [2]

Publication Abstract from PubMed

In Myxococcus xanthus, directed movement is controlled by pole-to-pole oscillations of the small GTPase MglA and its GAP MglB. Direction reversals require that MglA is inactivated by MglB, yet paradoxically MglA and MglB are located at opposite poles at reversal initiation. Here we report the complete MglA/MglB structural cycle combined to GAP kinetics and in vivo motility assays, which uncovers that MglA is a three-state GTPase and suggests a molecular mechanism for concerted MglA/MglB relocalizations. We show that MglA has an atypical GTP-bound state (MglA-GTP*) that is refractory to MglB and is re-sensitized by a feedback mechanism operated by MglA-GDP. By identifying and mutating the pole-binding region of MglB, we then provide evidence that the MglA-GTP* state exists in vivo. These data support a model in which MglA-GDP acts as a soluble messenger to convert polar MglA-GTP* into a diffusible MglA-GTP species that re-localizes to the opposite pole during reversals.

MglA functions as a three-state GTPase to control movement reversals of Myxococcus xanthus.,Galicia C, Lhospice S, Varela PF, Trapani S, Zhang W, Navaza J, Herrou J, Mignot T, Cherfils J Nat Commun. 2019 Nov 22;10(1):5300. doi: 10.1038/s41467-019-13274-3. PMID:31757955[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Spormann AM, Kaiser D. Gliding mutants of Myxococcus xanthus with high reversal frequencies and small displacements. J Bacteriol. 1999 Apr;181(8):2593-601. PMID:10198026
  2. Hartzell P, Kaiser D. Function of MglA, a 22-kilodalton protein essential for gliding in Myxococcus xanthus. J Bacteriol. 1991 Dec;173(23):7615-24. PMID:1938957
  3. Galicia C, Lhospice S, Varela PF, Trapani S, Zhang W, Navaza J, Herrou J, Mignot T, Cherfils J. MglA functions as a three-state GTPase to control movement reversals of Myxococcus xanthus. Nat Commun. 2019 Nov 22;10(1):5300. doi: 10.1038/s41467-019-13274-3. PMID:31757955 doi:http://dx.doi.org/10.1038/s41467-019-13274-3

6hjh, resolution 3.30Å

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