3ut6: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal structure of E. Coli PNP complexed with PO4 and formycin A== | ==Crystal structure of E. Coli PNP complexed with PO4 and formycin A== | ||
<StructureSection load='3ut6' size='340' side='right' caption='[[3ut6]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='3ut6' size='340' side='right' caption='[[3ut6]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| Line 6: | Line 7: | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3onv|3onv]], [[3ooe|3ooe]], [[3ooh|3ooh]], [[3opv|3opv]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3onv|3onv]], [[3ooe|3ooe]], [[3ooh|3ooh]], [[3opv|3opv]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Purine-nucleoside_phosphorylase Purine-nucleoside phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.1 2.4.2.1] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Purine-nucleoside_phosphorylase Purine-nucleoside phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.1 2.4.2.1] </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=3ut6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ut6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ut6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ut6 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=3ut6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ut6 OCA], [http://pdbe.org/3ut6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ut6 RCSB], [http://www.ebi.ac.uk/pdbsum/3ut6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ut6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| Line 18: | Line 19: | ||
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 3ut6" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 02:57, 5 August 2016
Crystal structure of E. Coli PNP complexed with PO4 and formycin ACrystal structure of E. Coli PNP complexed with PO4 and formycin A
Structural highlights
Function[DEOD_ECOLI] Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules.[HAMAP-Rule:MF_01627] Publication Abstract from PubMedPurine nucleoside phosphorylase (PNP) from Escherichia coli is a homohexamer that catalyses the phosphorolytic cleavage of the glycosidic bond of purine nucleosides. The first crystal structure of the ternary complex of this enzyme (with a phosphate ion and formycin A), which is biased by neither the presence of an inhibitor nor sulfate as a precipitant, is presented. The structure reveals, in some active sites, an unexpected and never before observed binding site for phosphate and exhibits a stoichiometry of two phosphate molecules per enzyme subunit. Moreover, in these active sites, the phosphate and nucleoside molecules are found not to be in direct contact. Rather, they are bridged by three water molecules that occupy the "standard" phosphate binding site. New phosphate binding sites in the crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with phosphate and formycin A.,Stefanic Z, Narczyk M, Mikleusevic G, Wielgus-Kutrowska B, Bzowska A, Luic M FEBS Lett. 2012 Apr 5;586(7):967-71. Epub 2012 Mar 1. PMID:22569248[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||||||