3t1v: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| (One intermediate revision by the same user not shown) | |||
| Line 1: | Line 1: | ||
==MglA bound to GDP in P2(1) tetrameric arrangement== | ==MglA bound to GDP in P2(1) tetrameric arrangement== | ||
<StructureSection load='3t1v' size='340' side='right' caption='[[3t1v]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='3t1v' size='340' side='right'caption='[[3t1v]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3t1v]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3t1v]] 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=3T1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T1V 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id=' | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3t1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t1v OCA], [https://pdbe.org/3t1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t1v RCSB], [https://www.ebi.ac.uk/pdbsum/3t1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t1v ProSAT]</span></td></tr> | ||
< | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5SJ82_THET8 Q5SJ82_THET8] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
| Line 20: | Line 19: | ||
</div> | </div> | ||
<div class="pdbe-citations 3t1v" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3t1v" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Gliding protein|Gliding protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Thermus thermophilus HB8]] | ||
[[Category: Koerner | [[Category: Koerner C]] | ||
[[Category: Miertzschke | [[Category: Miertzschke M]] | ||
[[Category: Vetter | [[Category: Vetter IR]] | ||
[[Category: Wittinghofer | [[Category: Wittinghofer A]] | ||
Latest revision as of 12:42, 30 October 2024
MglA bound to GDP in P2(1) tetrameric arrangementMglA bound to GDP in P2(1) tetrameric arrangement
Structural highlights
FunctionPublication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||