4rh0: Difference between revisions
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''' | ==Spore photoproduct lyase C140A/S76C mutant with bound AdoMet== | ||
<StructureSection load='4rh0' size='340' side='right' caption='[[4rh0]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4rh0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RH0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RH0 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fhc|4fhc]], [[4fhd|4fhd]], [[4fhe|4fhe]], [[4fhf|4fhf]], [[4fhg|4fhg]], [[4k9r|4k9r]], [[4rh1|4rh1]]</td></tr> | |||
<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> | |||
<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=4rh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rh0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4rh0 RCSB], [http://www.ebi.ac.uk/pdbsum/4rh0 PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Spore photoproduct lyase]] | |||
[[Category: Benjdia, A.]] | |||
[[Category: Carell, T.]] | |||
[[Category: Heil, K.]] | |||
[[Category: Schlichting, I.]] | |||
[[Category: Winkler, A.]] | |||
[[Category: Dna lyase]] | |||
[[Category: Dna repair]] | |||
[[Category: Lyase]] | |||
[[Category: Radical adomet enzyme]] | |||
[[Category: Radical sam enzyme]] | |||
[[Category: Tim barrel]] | |||
Revision as of 11:47, 22 October 2014
Spore photoproduct lyase C140A/S76C mutant with bound AdoMet
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