5br4: Difference between revisions

← Older edit

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5br4 is ON HOLD
+==E. coli lactaldehyde reductase (FucO) M185C mutant==
+<StructureSection load='5br4' size='340' side='right'caption='[[5br4]], [[Resolution|resolution]] 0.91&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5br4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BR4 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]] 0.91&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5br4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5br4 OCA], [https://pdbe.org/5br4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5br4 RCSB], [https://www.ebi.ac.uk/pdbsum/5br4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5br4 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FUCO_ECOLI FUCO_ECOLI]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+NAD(P)H-dependent enzymes are ubiquitous in metabolism and cellular processes and are also of great interest for pharmaceutical and industrial applications. Here, we present a structure-guided enzyme engineering strategy for improving catalytic properties of NAD(P)H-dependent enzymes toward native or native-like reactions using mutations to the enzyme's adenine-binding pocket, distal to the site of catalysis. Screening single-site saturation mutagenesis libraries identified mutations that increased catalytic efficiency up to 10-fold in 7 out of 10 enzymes. The enzymes improved in this study represent three different cofactor-binding folds (Rossmann, DHQS-like, and FAD/NAD binding) and utilize both NADH and NADPH. Structural and biochemical analyses show that the improved activities are accompanied by minimal changes in other properties (cooperativity, thermostability, pH optimum, uncoupling), and initial tests on two enzymes (ScADH6 and EcFucO) show improved functionality in Escherichia coli.
-Authors: Cahn, J.K.B., Brinkmann-Chen, S., Arnold, F.H.
+Mutations in adenine-binding pockets enhance catalytic properties of NAD(P)H-dependent enzymes.,Cahn JK, Baumschlager A, Brinkmann-Chen S, Arnold FH Protein Eng Des Sel. 2016 Jan;29(1):31-8. doi: 10.1093/protein/gzv057. Epub 2015 , Oct 27. PMID:26512129<ref>PMID:26512129</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Brinkmann-Chen, S]]
+<div class="pdbe-citations 5br4" style="background-color:#fffaf0;"></div>
-[[Category: Cahn, J.K.B]]
+== References ==
-[[Category: Arnold, F.H]]
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Escherichia coli]]
+[[Category: Large Structures]]
+[[Category: Arnold FH]]
+[[Category: Brinkmann-Chen S]]
+[[Category: Cahn JKB]]