View source for 2mja


==Solution Structure of Domain-Swapped GLPG==
<StructureSection load='2mja' size='340' side='right'caption='[[2mja]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mja]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MJA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MJA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mja FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mja OCA], [https://pdbe.org/2mja PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mja RCSB], [https://www.ebi.ac.uk/pdbsum/2mja PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mja ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/E2QFS2_ECOLX E2QFS2_ECOLX] Rhomboid-type serine protease that catalyzes intramembrane proteolysis.[HAMAP-Rule:MF_01594]
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== Publication Abstract from PubMed ==
Three-dimensional domain swapping is a mode of self-interaction that can give rise to altered functional states and has been identified as the trigger event in some protein deposition diseases, yet rates of interconversion between oligomeric states are usually slow, with the requirement for transient disruption of an extensive network of interactions giving rise to a large kinetic barrier. Here we demonstrate that the cytoplasmic domain of the Escherichia coli GlpG rhomboid protease undergoes slow dimerization via domain swapping and that micromolar concentrations of micelles can be used to enhance monomer-dimer exchange rates by more than 1000-fold. Detergents bearing a phosphocholine headgroup are shown to be true catalysts, with hexadecylphosphocholine reducing the 26 kcal/mol free energy barrier by &gt;11 kcal/mol while preserving the 5 kcal/mol difference between monomer and dimer states. Catalysis involves the formation of a micelle-bound intermediate with a partially unfolded structure that is primed for domain swapping. Taken together, these results are the first to demonstrate true catalysis for domain swapping, by using micelles that work in a chaperonin-like fashion to unfold a kinetically trapped state and allow access to the domain-swapped form.

Micelle-catalyzed domain swapping in the GlpG rhomboid protease cytoplasmic domain.,Ghasriani H, Kwok JK, Sherratt AR, Foo AC, Qureshi T, Goto NK Biochemistry. 2014 Sep 23;53(37):5907-15. doi: 10.1021/bi500919v. Epub 2014 Sep, 10. PMID:25162988<ref>PMID:25162988</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2mja" style="background-color:#fffaf0;"></div>

==See Also==
*[[Rhomboid protease|Rhomboid protease]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Ghasriani H]]
[[Category: Goto NK]]
[[Category: Kwok JKC]]
[[Category: Sherrat AR]]