7ct3: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal Structure of MglC from Myxococcus xanthus== | ==Crystal Structure of MglC from Myxococcus xanthus== | ||
<StructureSection load='7ct3' size='340' side='right'caption='[[7ct3]]' scene=''> | <StructureSection load='7ct3' size='340' side='right'caption='[[7ct3]], [[Resolution|resolution]] 1.85Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CT3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ct3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Myxxd Myxxd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7CT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7CT3 FirstGlance]. <br> | ||
</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=7ct3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ct3 OCA], [https://pdbe.org/7ct3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ct3 RCSB], [https://www.ebi.ac.uk/pdbsum/7ct3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ct3 ProSAT]</span></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MXAN_5770 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246197 MYXXD])</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=7ct3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ct3 OCA], [https://pdbe.org/7ct3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ct3 RCSB], [https://www.ebi.ac.uk/pdbsum/7ct3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ct3 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The delta-proteobacteria Myxococcus xanthus displays social (S) and adventurous (A) motilities, which require pole-to-pole reversal of the motility regulator proteins. Mutual gliding motility protein C (MglC), a paralog of GTPase-activating protein Mutual gliding motility protein B (MglB), is a member of the polarity module involved in regulating motility. However, little is known about the structure and function of MglC. Here, we determined approximately 1.85 A resolution crystal structure of MglC using Selenomethionine Single-wavelength anomalous diffraction. The crystal structure revealed that, despite sharing <9% sequence identity, both MglB and MglC adopt a Regulatory Light Chain 7 family fold. However, MglC has a distinct approximately 30 degrees to 40 degrees shift in the orientation of the functionally important alpha2 helix compared with other structural homologs. Using isothermal titration calorimetry and size-exclusion chromatography, we show that MglC binds MglB in 2:4 stoichiometry with submicromolar range dissociation constant. Using small-angle X-ray scattering and molecular docking studies, we show that the MglBC complex consists of a MglC homodimer sandwiched between two homodimers of MglB. A combination of size-exclusion chromatography and site-directed mutagenesis studies confirmed the MglBC interacting interface obtained by molecular docking studies. Finally, we show that the C-terminal region of MglB, crucial for binding its established partner MglA, is not required for binding MglC. These studies suggest that the MglB uses distinct interfaces to bind MglA and MglC. Based on these data, we propose a model suggesting a new role for MglC in polarity reversal in M. xanthus. | |||
Structural characterization of Myxococcus xanthus MglC, a component of the polarity control system, and its interactions with its paralog MglB.,Kapoor S, Kodesia A, Kalidas N, Ashish, Thakur KG J Biol Chem. 2021 Jan-Jun;296:100308. doi: 10.1016/j.jbc.2021.100308. Epub 2021, Jan 22. PMID:33493516<ref>PMID:33493516</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7ct3" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kapoor S]] | [[Category: Myxxd]] | ||
[[Category: Kodesia A]] | [[Category: Kapoor, S]] | ||
[[Category: Thakur | [[Category: Kodesia, A]] | ||
[[Category: Thakur, K G]] | |||
[[Category: Cytosolic protein]] | |||
[[Category: Roadblock/lc7 domain]] | |||
Revision as of 13:05, 14 July 2021
Crystal Structure of MglC from Myxococcus xanthusCrystal Structure of MglC from Myxococcus xanthus
Structural highlights
Publication Abstract from PubMedThe delta-proteobacteria Myxococcus xanthus displays social (S) and adventurous (A) motilities, which require pole-to-pole reversal of the motility regulator proteins. Mutual gliding motility protein C (MglC), a paralog of GTPase-activating protein Mutual gliding motility protein B (MglB), is a member of the polarity module involved in regulating motility. However, little is known about the structure and function of MglC. Here, we determined approximately 1.85 A resolution crystal structure of MglC using Selenomethionine Single-wavelength anomalous diffraction. The crystal structure revealed that, despite sharing <9% sequence identity, both MglB and MglC adopt a Regulatory Light Chain 7 family fold. However, MglC has a distinct approximately 30 degrees to 40 degrees shift in the orientation of the functionally important alpha2 helix compared with other structural homologs. Using isothermal titration calorimetry and size-exclusion chromatography, we show that MglC binds MglB in 2:4 stoichiometry with submicromolar range dissociation constant. Using small-angle X-ray scattering and molecular docking studies, we show that the MglBC complex consists of a MglC homodimer sandwiched between two homodimers of MglB. A combination of size-exclusion chromatography and site-directed mutagenesis studies confirmed the MglBC interacting interface obtained by molecular docking studies. Finally, we show that the C-terminal region of MglB, crucial for binding its established partner MglA, is not required for binding MglC. These studies suggest that the MglB uses distinct interfaces to bind MglA and MglC. Based on these data, we propose a model suggesting a new role for MglC in polarity reversal in M. xanthus. Structural characterization of Myxococcus xanthus MglC, a component of the polarity control system, and its interactions with its paralog MglB.,Kapoor S, Kodesia A, Kalidas N, Ashish, Thakur KG J Biol Chem. 2021 Jan-Jun;296:100308. doi: 10.1016/j.jbc.2021.100308. Epub 2021, Jan 22. PMID:33493516[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||||