4brp: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Legionella pneumophila NTPDase1 crystal form V (part-open)== | ==Legionella pneumophila NTPDase1 crystal form V (part-open)== | ||
<StructureSection load='4brp' size='340' side='right' caption='[[4brp]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='4brp' size='340' side='right' caption='[[4brp]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
| Line 6: | Line 7: | ||
<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]], [[4bre|4bre]], [[4brf|4brf]], [[4brg|4brg]], [[4brh|4brh]], [[4bri|4bri]], [[4brk|4brk]], [[4brl|4brl]], [[4brm|4brm]], [[4brn|4brn]], [[4bro|4bro]], [[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]], [[4bre|4bre]], [[4brf|4brf]], [[4brg|4brg]], [[4brh|4brh]], [[4bri|4bri]], [[4brk|4brk]], [[4brl|4brl]], [[4brm|4brm]], [[4brn|4brn]], [[4bro|4bro]], [[4brq|4brq]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Apyrase Apyrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.5 3.6.1.5] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Apyrase Apyrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.5 3.6.1.5] </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=4brp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4brp OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4brp RCSB], [http://www.ebi.ac.uk/pdbsum/4brp 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=4brp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4brp OCA], [http://pdbe.org/4brp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4brp RCSB], [http://www.ebi.ac.uk/pdbsum/4brp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4brp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
| Line 16: | Line 17: | ||
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 4brp" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Ectonucleoside triphosphate diphosphohydrolase|Ectonucleoside triphosphate diphosphohydrolase]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 11:48, 11 August 2016
Legionella pneumophila NTPDase1 crystal form V (part-open)Legionella pneumophila NTPDase1 crystal form V (part-open)
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
|
| ||||||||||||||||||||