5y9o

The apo structure of Legionella pneumophila WipA

spinqualitylabelsall models 5y9o, resolution 2.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5y9o is a 2 chain structure with sequence from Legionella pneumophila. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.554Å Ligands: IOD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5GA16_LEGPN Publication Abstract from PubMed The gram-negative bacterium Legionella pneumophila invades human's lung and causes Legionnaires' disease. To benefit its survival and replication in cellular milieu, L. pneumophila secrets at least 330 effector proteins into host cells. We found that the effector WipA has the protein tyrosine phosphatase (PTP) activity but does not depend on the classical CX5R motif for activity, suggesting that WipA is an unconventional PTP. Meanwhile, the presence of three other highly conserved motifs typically seen in protein serine/threonine phosphatases and the poor inhibition of WipA activity by okadaic acid led us to propose that WipA is a bacterial protein phosphatase. In addition, the determination of the 2.55-A crystal structure of WipA revealed that WipA resembles cold-active protein tyrosine phosphatase (CAPTPase), and therefore very likely shares the same catalytic mechanism. Legionella pneumophila effector WipA, a bacterial PPP protein phosphatase with PTP activity.,Jia Q, Lin Y, Gou X, He L, Shen D, Chen D, Xie W, Lu Y Acta Biochim Biophys Sin (Shanghai). 2018 Apr 26. pii: 4986413. doi:, 10.1093/abbs/gmy042. PMID:29701815 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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