3ooe: Difference between revisions
New page: '''Unreleased structure''' The entry 3ooe is ON HOLD Authors: Mikleusevic, G., Stefanic, Z., Narzyk, M., Wielgus-Kutrowska, B., Bzowska, A., Luic, M. Description: Crystal structure of ... |
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The | ==Crystal structure of E. Coli purine nucleoside phosphorylase with PO4== | ||
<StructureSection load='3ooe' size='340' side='right'caption='[[3ooe]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3ooe]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OOE FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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=3ooe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ooe OCA], [https://pdbe.org/3ooe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ooe RCSB], [https://www.ebi.ac.uk/pdbsum/3ooe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ooe ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/DEOD_ECOLI DEOD_ECOLI] Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules.[HAMAP-Rule:MF_01627] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The catalytic mechanism of Escherichia coli purine nucleoside phosphorylase (PNP) is revised using site-directed mutagenesis, kinetic studies and structure determinations. The experimental evidence on the role of the particular catalytic amino acid during catalysis has not been available. Therefore, the active site mutants Arg24Ala, Asp204Ala, Asp204Asn, Arg217Ala and Asp204Ala/Arg217Ala were prepared and their kinetics and thermodynamic studies were carried out. The activity tests with natural substrates and 7-methylguanosine confirmed the earlier hypothesis, that catalysis involves protonation of the purine base at position N7 by Asp204, which is triggered by Arg217. The crystal structures of the wild type in complexes with phosphate and sulphate, respectively, and of the Arg24Ala mutant in complex with phosphate/sulphate were determined. The structural data show that previously observed conformational change is a result of the phosphate binding and its interaction with Arg24. As E. coli PNP is a promising candidate for the tumour-directed gene therapy, our results may also help to design efficient mutants useful in gene therapy. | |||
Validation of the catalytic mechanism of Escherichiacoli purine nucleoside phosphorylase by structural and kinetic studies.,Mikleusevic G, Stefanic Z, Narczyk M, Wielgus-Kutrowska B, Bzowska A, Luic M Biochimie. 2011 Jun 13. PMID:21672603<ref>PMID:21672603</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3ooe" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Purine nucleoside phosphorylase 3D structures|Purine nucleoside phosphorylase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli K-12]] | |||
[[Category: Large Structures]] | |||
[[Category: Bzowska A]] | |||
[[Category: Luic M]] | |||
[[Category: Mikleusevic G]] | |||
[[Category: Narzyk M]] | |||
[[Category: Stefanic Z]] | |||
[[Category: Wielgus-Kutrowska B]] | |||
Latest revision as of 19:56, 1 November 2023
Crystal structure of E. Coli purine nucleoside phosphorylase with PO4Crystal structure of E. Coli purine nucleoside phosphorylase with PO4
Structural highlights
FunctionDEOD_ECOLI Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules.[HAMAP-Rule:MF_01627] Publication Abstract from PubMedThe catalytic mechanism of Escherichia coli purine nucleoside phosphorylase (PNP) is revised using site-directed mutagenesis, kinetic studies and structure determinations. The experimental evidence on the role of the particular catalytic amino acid during catalysis has not been available. Therefore, the active site mutants Arg24Ala, Asp204Ala, Asp204Asn, Arg217Ala and Asp204Ala/Arg217Ala were prepared and their kinetics and thermodynamic studies were carried out. The activity tests with natural substrates and 7-methylguanosine confirmed the earlier hypothesis, that catalysis involves protonation of the purine base at position N7 by Asp204, which is triggered by Arg217. The crystal structures of the wild type in complexes with phosphate and sulphate, respectively, and of the Arg24Ala mutant in complex with phosphate/sulphate were determined. The structural data show that previously observed conformational change is a result of the phosphate binding and its interaction with Arg24. As E. coli PNP is a promising candidate for the tumour-directed gene therapy, our results may also help to design efficient mutants useful in gene therapy. Validation of the catalytic mechanism of Escherichiacoli purine nucleoside phosphorylase by structural and kinetic studies.,Mikleusevic G, Stefanic Z, Narczyk M, Wielgus-Kutrowska B, Bzowska A, Luic M Biochimie. 2011 Jun 13. PMID:21672603[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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