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3AAR

Crystal structure of Lp1NTPDase from Legionella pneumophila in complex with AMPPNP

Summary for 3AAR
Entry DOI10.2210/pdb3aar/pdb
Related3AAP 3AAQ
DescriptorEctonucleoside triphosphate diphosphohydrolase I, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total)
Functional Keywordsadenosine triphosphatase, ntpdase, hydrolase
Biological sourceLegionella pneumophila
Total number of polymer chains1
Total formula weight40538.82
Authors
Ge, H.,Vivian, J.P.,Beddoe, T.,Rossjohn, J. (deposition date: 2009-11-24, release date: 2010-02-09, Last modification date: 2024-10-30)
Primary citationVivian, J.P.,Riedmaier, P.,Ge, H.,Le Nours, J.,Sansom, F.M.,Wilce, M.C.J.,Byres, E.,Dias, M.,Schmidberger, J.W.,Cowan, P.J.,d'Apice, A.J.F.,Hartland, E.L.,Rossjohn, J.,Beddoe, T.
Crystal Structure of a Legionella pneumophila Ecto -Triphosphate Diphosphohydrolase, A Structural and Functional Homolog of the Eukaryotic NTPDases
Structure, 18:228-238, 2010
Cited by
PubMed Abstract: Many pathogenic bacteria have sophisticated mechanisms to interfere with the mammalian immune response. These include the disruption of host extracellular ATP levels that, in humans, is tightly regulated by the nucleoside triphosphate diphosphohydrolase family (NTPDases). NTPDases are found almost exclusively in eukaryotes, the notable exception being their presence in some pathogenic prokaryotes. To address the function of bacterial NTPDases, we describe the structures of an NTPDase from the pathogen Legionella pneumophila (Lpg1905/Lp1NTPDase) in its apo state and in complex with the ATP analog AMPPNP and the subtype-specific NTPDase inhibitor ARL 67156. Lp1NTPDase is structurally and catalytically related to eukaryotic NTPDases and the structure provides a basis for NTPDase-specific inhibition. Furthermore, we demonstrate that the activity of Lp1NTPDase correlates directly with intracellular replication of Legionella within macrophages. Collectively, these findings provide insight into the mechanism of this enzyme and highlight its role in host-pathogen interactions.
PubMed: 20159467
DOI: 10.1016/j.str.2009.11.014
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.65 Å)
Structure validation

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