6izw: Difference between revisions
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<StructureSection load='6izw' size='340' side='right'caption='[[6izw]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='6izw' size='340' side='right'caption='[[6izw]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6izw]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IZW OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6izw]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxococcus_xanthus_DK_1622 Myxococcus xanthus DK 1622]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6IZW FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GSP:5-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE'>GSP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6izw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6izw OCA], [https://pdbe.org/6izw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6izw RCSB], [https://www.ebi.ac.uk/pdbsum/6izw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6izw ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6izw" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6izw" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Gliding protein|Gliding protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Myxococcus xanthus DK 1622]] | ||
[[Category: Baranwal | [[Category: Baranwal J]] | ||
[[Category: Gayathri | [[Category: Gayathri P]] | ||
Latest revision as of 12:56, 22 November 2023
Myxococcus xanthus MglA bound to GTP-gamma-S and MglBMyxococcus xanthus MglA bound to GTP-gamma-S and MglB
Structural highlights
FunctionMGLA_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 PubMedMutual 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. Allosteric regulation of a prokaryotic small Ras-like GTPase contributes to cell polarity oscillations in bacterial motility.,Baranwal J, Lhospice S, Kanade M, Chakraborty S, Gade PR, Harne S, Herrou J, Mignot T, Gayathri P PLoS Biol. 2019 Sep 27;17(9):e3000459. doi: 10.1371/journal.pbio.3000459., eCollection 2019 Sep. PMID:31560685[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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