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3uaz

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==Crystal structure of Bacillus cereus adenosine phosphorylase D204N mutant complexed with inosine==
==Crystal structure of Bacillus cereus adenosine phosphorylase D204N mutant complexed with inosine==
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<StructureSection load='3uaz' size='340' side='right' caption='[[3uaz]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
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<StructureSection load='3uaz' size='340' side='right'caption='[[3uaz]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3uaz]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_14579 Atcc 14579]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UAZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UAZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3uaz]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UAZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UAZ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NOS:INOSINE'>NOS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3uav|3uav]], [[3uaw|3uaw]], [[3uax|3uax]], [[3uay|3uay]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NOS:INOSINE'>NOS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">deoD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 ATCC 14579])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3uaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uaz OCA], [https://pdbe.org/3uaz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uaz RCSB], [https://www.ebi.ac.uk/pdbsum/3uaz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uaz ProSAT]</span></td></tr>
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<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>
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<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=3uaz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uaz OCA], [http://pdbe.org/3uaz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3uaz RCSB], [http://www.ebi.ac.uk/pdbsum/3uaz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3uaz ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/DEOD_BACCE DEOD_BACCE]
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Purine nucleoside phosphorylases catalyze the phosphorolytic cleavage of the glycosidic bond of purine (2'-deoxy)nucleosides, generating the corresponding free base and (2'-deoxy)ribose 1-phosphate. Two classes of PNPs have been identified: homotrimers specific for 6-oxopurines and homohexamers that accept both 6-oxopurines and 6-aminopurines. Bacillus cereus adenosine phosphorylase (AdoP) is a hexameric PNP; however, it is highly specific for 6-aminopurines. To investigate the structural basis for the unique substrate specificity of AdoP, the active-site mutant D204N was prepared and kinetically characterized and the structures of the wild-type protein and the D204N mutant complexed with adenosine and sulfate or with inosine and sulfate were determined at high resolution (1.2-1.4 A). AdoP interacts directly with the preferred substrate through a hydrogen-bond donation from the catalytically important residue Asp204 to N7 of the purine base. Comparison with Escherichia coli PNP revealed a more optimal orientation of Asp204 towards N7 of adenosine and a more closed active site. When inosine is bound, two water molecules are interposed between Asp204 and the N7 and O6 atoms of the nucleoside, thus allowing the enzyme to find alternative but less efficient ways to stabilize the transition state. The mutation of Asp204 to asparagine led to a significant decrease in catalytic efficiency for adenosine without affecting the efficiency of inosine cleavage.
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Structural basis of the substrate specificity of Bacillus cereus adenosine phosphorylase.,Dessanti P, Zhang Y, Allegrini S, Tozzi MG, Sgarrella F, Ealick SE Acta Crystallogr D Biol Crystallogr. 2012 Mar;68(Pt 3):239-48. Epub 2012 Feb 14. PMID:22349225<ref>PMID:22349225</ref>
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==See Also==
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*[[Purine nucleoside phosphorylase 3D structures|Purine nucleoside phosphorylase 3D structures]]
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3uaz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 14579]]
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[[Category: Bacillus cereus]]
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[[Category: Purine-nucleoside phosphorylase]]
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[[Category: Large Structures]]
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[[Category: Allegrini, S]]
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[[Category: Allegrini S]]
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[[Category: Dessanti, P]]
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[[Category: Dessanti P]]
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[[Category: Ealick, S E]]
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[[Category: Ealick SE]]
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[[Category: Sgarrella, F]]
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[[Category: Sgarrella F]]
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[[Category: Tozzi, M G]]
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[[Category: Tozzi MG]]
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[[Category: Zhang, Y]]
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[[Category: Zhang Y]]
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[[Category: Transferase]]
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Current revision

Crystal structure of Bacillus cereus adenosine phosphorylase D204N mutant complexed with inosine

PDB ID 3uaz

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