4f60
From Proteopedia
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| - | [[ | + | ==Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (T148L, G171Q, A172V, C176F).== |
| + | <StructureSection load='4f60' size='340' side='right' caption='[[4f60]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4f60]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodococcus_rhodochrous Rhodococcus rhodochrous]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F60 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4F60 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=F:FLUORIDE+ION'>F</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">dhaA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1829 Rhodococcus rhodochrous])</td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Haloalkane_dehalogenase Haloalkane dehalogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.8.1.5 3.8.1.5] </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=4f60 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f60 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4f60 RCSB], [http://www.ebi.ac.uk/pdbsum/4f60 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Mutations targeting as few as four residues lining the access tunnel extended the half-life of an enzyme in 40 % dimethyl sulfoxide from minutes to weeks and increased its melting temperature by 190 degrees C. Protein crystallography and molecular dynamics revealed that the tunnel residue packing is a key determinant of protein stability and the active-site accessibility for cosolvent molecules (red dots). | ||
| - | + | Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel.,Koudelakova T, Chaloupkova R, Brezovsky J, Prokop Z, Sebestova E, Hesseler M, Khabiri M, Plevaka M, Kulik D, Kuta Smatanova I, Rezacova P, Ettrich R, Bornscheuer UT, Damborsky J Angew Chem Int Ed Engl. 2013 Jan 9. doi: 10.1002/anie.201206708. PMID:23303607<ref>PMID:23303607</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| - | + | ==See Also== | |
| - | + | *[[Dehalogenase|Dehalogenase]] | |
| - | == | + | == References == |
| - | [[ | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Haloalkane dehalogenase]] | [[Category: Haloalkane dehalogenase]] | ||
[[Category: Rhodococcus rhodochrous]] | [[Category: Rhodococcus rhodochrous]] | ||
| - | [[Category: Kuta-Smatanova, I | + | [[Category: Kuta-Smatanova, I]] |
| - | [[Category: Plevaka, M | + | [[Category: Plevaka, M]] |
| - | [[Category: Rezacova, P | + | [[Category: Rezacova, P]] |
[[Category: Hydrolase]] | [[Category: Hydrolase]] | ||
[[Category: Mutation in access tunnel]] | [[Category: Mutation in access tunnel]] | ||
Revision as of 17:07, 9 December 2014
Crystal structure of Rhodococcus rhodochrous haloalkane dehalogenase mutant (T148L, G171Q, A172V, C176F).
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