5g4k
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5g4k is ON HOLD until Paper Publication Authors: Conradt, D., Hermann, B., Gerhardt, S., Einsle, O., Mueller, M. Description: Phloroglucinol reduct...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Phloroglucinol reductase from Clostridium sp. apo-form== | |
| + | <StructureSection load='5g4k' size='340' side='right'caption='[[5g4k]], [[Resolution|resolution]] 1.74Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5g4k]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_sp. Clostridium sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5G4K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5G4K 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]] 1.74Å</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=5g4k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5g4k OCA], [https://pdbe.org/5g4k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5g4k RCSB], [https://www.ebi.ac.uk/pdbsum/5g4k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5g4k ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Phloroglucinol reductases (PGRs) are involved in anaerobic degradation in bacteria, in which they catalyze the dearomatization of phloroglucinol into dihydrophloroglucinol. We identified three PGRs, from different bacterial species, that are members of the family of NAD(P)H-dependent short-chain dehydrogenases/reductases (SDRs). In addition to catalyzing the reduction of the physiological substrate, the three enzymes exhibit activity towards 2,4,6-trihydroxybenzaldehyde, 2,4,6-trihydroxyacetophenone, and methyl 2,4,6-trihydroxybenzoate. Structural elucidation of PGRcl and comparison to known SDRs revealed a high degree of conservation. Several amino acid positions were identified as being conserved within the PGR subfamily and might be involved in substrate differentiation. The results enable the enzymatic dearomatization of monoaromatic phenol derivatives and provide insight into the functional diversity that may be found in families of enzymes displaying a high degree of structural homology. | ||
| - | + | Biocatalytic Properties and Structural Analysis of Phloroglucinol Reductases.,Conradt D, Hermann B, Gerhardt S, Einsle O, Muller M Angew Chem Int Ed Engl. 2016 Dec 12;55(50):15531-15534. doi:, 10.1002/anie.201607494. Epub 2016 Nov 22. PMID:27874239<ref>PMID:27874239</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5g4k" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Gerhardt | + | <references/> |
| - | [[Category: | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Clostridium sp]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Conradt D]] | ||
| + | [[Category: Einsle O]] | ||
| + | [[Category: Gerhardt S]] | ||
| + | [[Category: Hermann B]] | ||
| + | [[Category: Mueller M]] | ||
Current revision
Phloroglucinol reductase from Clostridium sp. apo-form
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