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==Legionella pneumophila NTPDase1 crystal form II (closed) in complex with transition state mimic adenosine 5'phosphovanadate== | ==Legionella pneumophila NTPDase1 crystal form II (closed) in complex with transition state mimic adenosine 5'phosphovanadate== | ||
<StructureSection load='4bre' size='340' side='right' caption='[[4bre]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4bre' size='340' side='right' caption='[[4bre]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=50T:ADENOSINE-5-PHOSPHOVANADATE'>50T</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=50T:ADENOSINE-5-PHOSPHOVANADATE'>50T</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bqz|4bqz]], [[4br0|4br0]], [[4br2|4br2]], [[4br4|4br4]], [[4br5|4br5]], [[4br7|4br7]], [[4br9|4br9]], [[4bra|4bra]], [[4brc|4brc]], [[4brd|4brd]], [[4brf|4brf]], [[4brg|4brg]], [[4brh|4brh]], [[4bri|4bri]], [[4brk|4brk]], [[4brl|4brl]], [[4brm|4brm]], [[4brn|4brn]], [[4bro|4bro]], [[4brp|4brp]], [[4brq|4brq]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4bqz|4bqz]], [[4br0|4br0]], [[4br2|4br2]], [[4br4|4br4]], [[4br5|4br5]], [[4br7|4br7]], [[4br9|4br9]], [[4bra|4bra]], [[4brc|4brc]], [[4brd|4brd]], [[4brf|4brf]], [[4brg|4brg]], [[4brh|4brh]], [[4bri|4bri]], [[4brk|4brk]], [[4brl|4brl]], [[4brm|4brm]], [[4brn|4brn]], [[4bro|4bro]], [[4brp|4brp]], [[4brq|4brq]]</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=4bre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bre OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bre RCSB], [http://www.ebi.ac.uk/pdbsum/4bre PDBsum]</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=4bre FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bre OCA], [http://pdbe.org/4bre PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bre RCSB], [http://www.ebi.ac.uk/pdbsum/4bre PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bre ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 4bre" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 13:17, 11 August 2016
Legionella pneumophila NTPDase1 crystal form II (closed) in complex with transition state mimic adenosine 5'phosphovanadateLegionella pneumophila NTPDase1 crystal form II (closed) in complex with transition state mimic adenosine 5'phosphovanadate
Structural highlights
Publication Abstract from PubMedIn vertebrates, membrane-bound ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) on the cell surface are responsible for signal conversion and termination in purinergic signaling by extracellular nucleotides. Here we present apo and complex structures of the rat NTPDase2 extracellular domain and Legionella pneumophila NTPDase1, including a high-resolution structure with a transition-state analog. Comparison of ATP and ADP binding modes shows how NTPDases engage the same catalytic site for hydrolysis of nucleoside triphosphates and diphosphates. We find that this dual specificity is achieved at the expense of base specificity. Structural and mutational studies indicate that a conserved active-site water is replaced by the phosphate product immediately after phosphoryl transfer. Partial base specificity for purines in LpNTPDase1 is based on a different intersubunit base binding site for pyrimidine bases. A comparison of the bacterial enzyme in six independent crystal forms shows that NTPDases can undergo a domain closure motion of at least 17 degrees . Crystallographic Snapshots along the Reaction Pathway of Nucleoside Triphosphate Diphosphohydrolases.,Zebisch M, Krauss M, Schafer P, Lauble P, Strater N Structure. 2013 Jul 2. pii: S0969-2126(13)00200-1. doi:, 10.1016/j.str.2013.05.016. PMID:23830739[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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