1poq

Solution Structure of a Superantigen from Yersinia pseudotuberculosis

spinqualitylabelsall models 1poq Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1poq is a 1 chain structure with sequence from Yersinia pseudotuberculosis. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q57221_YERPU Publication Abstract from PubMed Superantigens are a class of microbial proteins with the ability to excessively activate T cells by binding to the T cell receptor. The staphylococcal and streptococcal superantigens are closely related in structure and possess an N-terminal domain that resembles an OB fold and a C-terminal domain similar to a beta-grasp fold. Yersinia pseudotuberculosis produces superantigens, YPMa, YPMb, and YPMc, which have no significant amino acid similarity to other proteins. We have determined the crystal and solution structures of YPMa, which show that the protein has a jelly-roll fold. The closest structural neighbors to YPMa are viral capsid proteins and members of the tumor necrosis factor superfamily. In the crystal structure, YPMa packs as a trimer, another feature shared with viral capsid proteins and TNF superfamily proteins. However, in solution YPMa behaves as a monomer, and any functional relevance of the trimer observed in the crystals is yet to be established. Crystal and solution structures of a superantigen from Yersinia pseudotuberculosis reveal a jelly-roll fold.,Donadini R, Liew CW, Kwan AH, Mackay JP, Fields BA Structure. 2004 Jan;12(1):145-56. PMID:14725774 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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