4zxz
From Proteopedia
(Difference between revisions)
m (Protected "4zxz" [edit=sysop:move=sysop]) |
|||
| (4 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a highly thermal stable but inactive levoglucosan kinase.== | |
| + | <StructureSection load='4zxz' size='340' side='right'caption='[[4zxz]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4zxz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lipomyces_starkeyi Lipomyces starkeyi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZXZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZXZ 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]] 2.2Å</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=4zxz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zxz OCA], [https://pdbe.org/4zxz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zxz RCSB], [https://www.ebi.ac.uk/pdbsum/4zxz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zxz ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Synthetic metabolic pathways often suffer from low specific productivity, and new methods that quickly assess pathway functionality for many thousands of variants are urgently needed. Here we present an approach that enables the rapid and parallel determination of sequence effects on flux for complete gene-encoding sequences. We show that this method can be used to determine the effects of over 8000 single point mutants of a pyrolysis oil catabolic pathway implanted in Escherichia coli. Experimental sequence-function data sets predicted whether fitness-enhancing mutations to the enzyme levoglucosan kinase resulted from enhanced catalytic efficiency or enzyme stability. A structure of one design incorporating 38 mutations elucidated the structural basis of high fitness mutations. One design incorporating 15 beneficial mutations supported a 15-fold improvement in growth rate and greater than 24-fold improvement in enzyme activity relative to the starting pathway. This technique can be extended to improve a wide variety of designed pathways. | ||
| - | + | Comprehensive Sequence-Flux Mapping of a Levoglucosan Utilization Pathway in E. coli.,Klesmith JR, Bacik JP, Michalczyk R, Whitehead TA ACS Synth Biol. 2015 Sep 22. PMID:26369947<ref>PMID:26369947</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 4zxz" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lipomyces starkeyi]] | ||
| + | [[Category: Bacik JP]] | ||
| + | [[Category: Klesmith JR]] | ||
| + | [[Category: Whitehead TA]] | ||
Current revision
Crystal structure of a highly thermal stable but inactive levoglucosan kinase.
| |||||||||||
