2mja

Solution Structure of Domain-Swapped GLPG

spinqualitylabelsall models 2mja, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mja is a 2 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2lep Activity: Rhomboid protease, with EC number 3.4.21.105 Resources: FirstGlance, OCA, RCSB, PDBsum Function [E2QFS2_ECOLX] Rhomboid-type serine protease that catalyzes intramembrane proteolysis.[HAMAP-Rule:MF_01594] 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 >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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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