4br7: Difference between revisions
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==Legionella pneumophila NTPDase1 crystal form I, open, AMPNP complex== | ==Legionella pneumophila NTPDase1 crystal form I, open, AMPNP complex== | ||
<StructureSection load='4br7' size='340' side='right' caption='[[4br7]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='4br7' size='340' side='right'caption='[[4br7]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4br7]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4br7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BR7 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AU1:5-O-[(R)-HYDROXY(PHOSPHONOAMINO)PHOSPHORYL]ADENOSINE'>AU1</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AU1:5-O-[(R)-HYDROXY(PHOSPHONOAMINO)PHOSPHORYL]ADENOSINE'>AU1</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4br7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4br7 OCA], [https://pdbe.org/4br7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4br7 RCSB], [https://www.ebi.ac.uk/pdbsum/4br7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4br7 ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q5ZUA2_LEGPH Q5ZUA2_LEGPH] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Legionella pneumophila]] | ||
[[Category: Lauble | [[Category: Lauble P]] | ||
[[Category: Schaefer | [[Category: Schaefer P]] | ||
[[Category: Straeter | [[Category: Straeter N]] | ||
[[Category: Zebisch | [[Category: Zebisch M]] | ||
Latest revision as of 11:21, 23 October 2024
Legionella pneumophila NTPDase1 crystal form I, open, AMPNP complexLegionella pneumophila NTPDase1 crystal form I, open, AMPNP complex
Structural highlights
FunctionPublication 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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