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| | ==Crystal Structure of Lp1NTPDase from Legionella pneumophila== | | ==Crystal Structure of Lp1NTPDase from Legionella pneumophila== |
| - | <StructureSection load='3aap' size='340' side='right' caption='[[3aap]], [[Resolution|resolution]] 1.60Å' scene=''> | + | <StructureSection load='3aap' size='340' side='right'caption='[[3aap]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3aap]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Legph Legph]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AAP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3AAP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3aap]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._Philadelphia_1 Legionella pneumophila subsp. pneumophila str. Philadelphia 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3AAP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3AAP FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3aaq|3aaq]], [[3aar|3aar]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lpg1905 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=272624 LEGPH])</td></tr>
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3aap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aap OCA], [https://pdbe.org/3aap PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3aap RCSB], [https://www.ebi.ac.uk/pdbsum/3aap PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3aap ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3aap FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3aap OCA], [http://pdbe.org/3aap PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3aap RCSB], [http://www.ebi.ac.uk/pdbsum/3aap PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3aap ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q5ZUA2_LEGPH Q5ZUA2_LEGPH] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Legph]] | + | [[Category: Large Structures]] |
| - | [[Category: Beddoe, T]] | + | [[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]] |
| - | [[Category: Rossjohn, J]] | + | [[Category: Beddoe T]] |
| - | [[Category: Vivian, J P]] | + | [[Category: Rossjohn J]] |
| - | [[Category: Adenosine triphosphatase]] | + | [[Category: Vivian JP]] |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Ntpdase]]
| + | |
| Structural highlights
Function
Q5ZUA2_LEGPH
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Crystal structure of a Legionella pneumophila ecto -triphosphate diphosphohydrolase, a structural and functional homolog of the eukaryotic NTPDases.,Vivian JP, Riedmaier P, Ge H, Le Nours J, Sansom FM, Wilce MC, Byres E, Dias M, Schmidberger JW, Cowan PJ, d'Apice AJ, Hartland EL, Rossjohn J, Beddoe T Structure. 2010 Feb 10;18(2):228-38. PMID:20159467[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Vivian JP, Riedmaier P, Ge H, Le Nours J, Sansom FM, Wilce MC, Byres E, Dias M, Schmidberger JW, Cowan PJ, d'Apice AJ, Hartland EL, Rossjohn J, Beddoe T. Crystal structure of a Legionella pneumophila ecto -triphosphate diphosphohydrolase, a structural and functional homolog of the eukaryotic NTPDases. Structure. 2010 Feb 10;18(2):228-38. PMID:20159467 doi:10.1016/j.str.2009.11.014
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