5etj

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'''Unreleased structure'''
 
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The entry 5etj is ON HOLD until Paper Publication
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==Crystal structure of purine nucleoside phosphorylase (E258D, L261A) mutant from human complexed with DADMe-ImmG and phosphate==
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<StructureSection load='5etj' size='340' side='right' caption='[[5etj]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5etj]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ETJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ETJ 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=IM5:2-AMINO-7-{[(3R,4R)-3-HYDROXY-4-(HYDROXYMETHYL)PYRROLIDIN-1-YL]METHYL}-3,5-DIHYDRO-4H-PYRROLO[3,2-D]PYRIMIDIN-4-ONE'>IM5</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3phb|3phb]]</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=5etj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5etj OCA], [http://pdbe.org/5etj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5etj RCSB], [http://www.ebi.ac.uk/pdbsum/5etj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5etj ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/PNPH_HUMAN PNPH_HUMAN]] Defects in PNP are the cause of purine nucleoside phosphorylase deficiency (PNPD) [MIM:[http://omim.org/entry/613179 613179]]. It leads to a severe T-cell immunodeficiency with neurologic disorder in children.<ref>PMID:3029074</ref> <ref>PMID:1384322</ref> <ref>PMID:8931706</ref>
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== Function ==
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[[http://www.uniprot.org/uniprot/PNPH_HUMAN PNPH_HUMAN]] The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.<ref>PMID:2104852</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The relevance of sub-picosecond protein motions to the catalytic event remains a topic of debate. Heavy enzymes (isotopically substituted) provide an experimental tool for bond-vibrational links to enzyme catalysis. A recent transition path sampling study with heavy purine nucleoside phosphorylase (PNP) characterized the experimentally observed mass-dependent slowing of barrier crossing (Antoniou, D.; Ge, X.; Schramm, V. L.; Schwartz, S. D. J. Phys. Chem. Lett. 2012, 3, 3538). Here we computationally identify second-sphere amino acid residues predicted to influence the freedom of the catalytic site vibrational modes linked to heavy enzyme effects in PNP. We mutated heavy and light PNPs to increase the catalytic site vibrational freedom. Enzymatic barrier-crossing rates were converted from mass-dependent to mass-independent as a result of the mutations. The mutagenic uncoupling of femtosecond motions between catalytic site groups and reactants decreased transition state barrier crossing by 2 orders of magnitude, an indication of the femtosecond dynamic contributions to catalysis.
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Authors: Cameron, S.A., Suarez, J., Schramm, V.L., Almo, S.C.
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Modulating Enzyme Catalysis through Mutations Designed to Alter Rapid Protein Dynamics.,Zoi I, Suarez J, Antoniou D, Cameron SA, Schramm VL, Schwartz SD J Am Chem Soc. 2016 Mar 16;138(10):3403-9. doi: 10.1021/jacs.5b12551. Epub 2016, Mar 8. PMID:26927977<ref>PMID:26927977</ref>
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Description: Crystal structure of purine nucleoside phosphorylase (E258D, L261A) mutant from human complexed with DADMe-ImmG and phosphate
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Almo, S.C]]
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<div class="pdbe-citations 5etj" style="background-color:#fffaf0;"></div>
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[[Category: Schramm, V.L]]
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== References ==
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[[Category: Cameron, S.A]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Purine-nucleoside phosphorylase]]
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[[Category: Almo, S C]]
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[[Category: Cameron, S A]]
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[[Category: Schramm, V L]]
[[Category: Suarez, J]]
[[Category: Suarez, J]]
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[[Category: Phosphorylase]]
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[[Category: Transferase-transferase inhibitor complex]]

Revision as of 15:15, 14 September 2016

Crystal structure of purine nucleoside phosphorylase (E258D, L261A) mutant from human complexed with DADMe-ImmG and phosphate

5etj, resolution 2.30Å

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