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3t1r

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==MglB with tetrameric arrangement==
==MglB with tetrameric arrangement==
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<StructureSection load='3t1r' size='340' side='right' caption='[[3t1r]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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<StructureSection load='3t1r' size='340' side='right'caption='[[3t1r]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3t1r]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet8 Thet8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T1R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T1R FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3t1r]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB8 Thermus thermophilus HB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T1R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T1R FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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</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&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3t12|3t12]], [[3t1o|3t1o]], [[3t1q|3t1q]], [[3t1s|3t1s]], [[3t1t|3t1t]], [[3t1v|3t1v]], [[3t1x|3t1x]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TTHA1131 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=300852 THET8])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t1r OCA], [https://pdbe.org/3t1r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t1r RCSB], [https://www.ebi.ac.uk/pdbsum/3t1r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t1r ProSAT]</span></td></tr>
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<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=3t1r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t1r OCA], [http://pdbe.org/3t1r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t1r RCSB], [http://www.ebi.ac.uk/pdbsum/3t1r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t1r ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q5SJ83_THET8 Q5SJ83_THET8]
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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 beta2-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.
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Structural analysis of the Ras-like G protein MglA and its cognate GAP MglB and implications for bacterial polarity.,Miertzschke M, Koerner C, Vetter IR, Keilberg D, Hot E, Leonardy S, Sogaard-Andersen L, Wittinghofer A EMBO J. 2011 Aug 16. doi: 10.1038/emboj.2011.291. PMID:21847100<ref>PMID:21847100</ref>
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==See Also==
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*[[Gliding protein|Gliding protein]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3t1r" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Thet8]]
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[[Category: Large Structures]]
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[[Category: Koerner, C]]
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[[Category: Thermus thermophilus HB8]]
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[[Category: Miertzschke, M]]
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[[Category: Koerner C]]
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[[Category: Vetter, I R]]
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[[Category: Miertzschke M]]
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[[Category: Wittinghofer, A]]
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[[Category: Vetter IR]]
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[[Category: Alpha/beta protein]]
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[[Category: Wittinghofer A]]
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[[Category: Bacterial polarity and motility]]
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[[Category: Catalytic gap domain]]
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[[Category: Gtpase activating protein]]
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[[Category: Homodimer]]
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[[Category: Signaling protein]]
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[[Category: Signalling protein]]
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Current revision

MglB with tetrameric arrangement

PDB ID 3t1r

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