4rh1

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m (Protected "4rh1" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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==Spore photoproduct lyase C140A/S76C mutant with bound AdoMet and dinucleoside spore photoproduct==
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<StructureSection load='4rh1' size='340' side='right' caption='[[4rh1]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4rh1]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RH1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RH1 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=0TT:1-[(2R,4S,5R)-5-(HYDROXYMETHYL)-4-OXIDANYL-OXOLAN-2-YL]-5-[[(5R)-1-[(2R,4S,5R)-5-(HYDROXYMETHYL)-4-OXIDANYL-OXOLAN-2-YL]-5-METHYL-2,4-BIS(OXIDANYLIDENE)-1,3-DIAZINAN-5-YL]METHYL]PYRIMIDINE-2,4-DIONE'>0TT</scene>, <scene name='pdbligand=EEM:[(3S)-3-AMINO-4-HYDROXY-4-OXO-BUTYL]-[[(2S,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL]-METHYL-SELANIUM'>EEM</scene>, <scene name='pdbligand=SF4:IRON/SULFUR+CLUSTER'>SF4</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4rh0|4rh0]]</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/Spore_photoproduct_lyase Spore photoproduct lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.99.14 4.1.99.14] </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=4rh1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rh1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rh1 RCSB], [http://www.ebi.ac.uk/pdbsum/4rh1 PDBsum]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The radical SAM enzyme, spore photoproduct lyase, requires an H-atom transfer (HAT) pathway to catalyze DNA repair. By rational engineering, we demonstrate that it is possible to rewire its HAT pathway, a first step toward the development of novel catalysts based on the radical SAM enzyme scaffold.
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The entry 4rh1 is ON HOLD
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Rescuing DNA repair activity by rewiring the H-atom transfer pathway in the radical SAM enzyme, spore photoproduct lyase.,Benjdia A, Heil K, Winkler A, Carell T, Schlichting I Chem Commun (Camb). 2014 Oct 6. PMID:25285338<ref>PMID:25285338</ref>
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Authors: Benjdia, A., Heil, K., Winkler, A., Carell, T., Schlichting, I.
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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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Description: Spore photoproduct lyase C140A/S76C mutant with bound AdoMet and dinucleoside spore photoproduct
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Spore photoproduct lyase]]
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[[Category: Benjdia, A.]]
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[[Category: Carell, T.]]
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[[Category: Heil, K.]]
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[[Category: Schlichting, I.]]
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[[Category: Winkler, A.]]
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[[Category: Dna lyase]]
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[[Category: Dna repair]]
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[[Category: Lyase]]
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[[Category: Radical adomet enzyme]]
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[[Category: Radical sam enzyme]]
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[[Category: Tim barrel]]

Revision as of 11:47, 22 October 2014

Spore photoproduct lyase C140A/S76C mutant with bound AdoMet and dinucleoside spore photoproduct

4rh1, resolution 2.60Å

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