6nen | pdb_00006nen

Catalytic domain of Proteus mirabilis ScsC

spinqualitylabelsall models 6nen, resolution 2.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6nen is a 1 chain structure with sequence from Proteus mirabilis. This structure supersedes the now removed PDB entry 4yx8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.151Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B4EV21_PROMH Publication Abstract from PubMed Suppressor of copper sensitivity protein C from Proteus mirabilis (PmScsC) is a homotrimeric disulfide isomerase that plays a role in copper tolerance, which is a key virulence trait of this uropathogen. Each protomer of the enzyme has an N-terminal trimerization stem (59 residues) containing a flexible linker (11 residues) connected to a thioredoxin-fold-containing catalytic domain (163 residues). Here, two PmScsC variants, PmScsCDeltaN and PmScsCDeltaLinker, are characterized. PmScsCDeltaN is an N-terminally truncated form of the protomer with two helices of the trimerization stem removed, generating a protein with dithiol oxidase rather than disulfide isomerase activity. The crystal structure of PmScsCDeltaN reported here reveals, as expected, a monomer that is structurally similar to the catalytic domain of native PmScsC. The second variant, PmScsCDeltaLinker, was designed to remove the 11-amino-acid linker, and it is shown that it generates a protein that has neither disulfide isomerase nor dithiol oxidase activity. The crystal structure of PmScsCDeltaLinker reveals a trimeric arrangement, with the catalytic domains packed together very closely. Small-angle X-ray scattering analysis found that native PmScsC is predominantly trimeric in solution even at low concentrations, whereas PmScsCDeltaLinker exists as an equilibrium between monomeric, dimeric and trimeric states, with the monomeric form dominating at low concentrations. These findings increase the understanding of disulfide isomerase activity, showing how (i) oligomerization, (ii) the spacing between and (iii) the dynamic motion of catalytic domains in PmScsC all contribute to its native function. Engineered variants provide new insight into the structural properties important for activity of the highly dynamic, trimeric protein disulfide isomerase ScsC from Proteus mirabilis.,Furlong EJ, Kurth F, Premkumar L, Whitten AE, Martin JL Acta Crystallogr D Struct Biol. 2019 Mar 1;75(Pt 3):296-307. doi:, 10.1107/S2059798319000081. Epub 2019 Feb 26. PMID:30950400 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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