4k2a: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 8: | Line 8: | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k2a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k2a RCSB], [http://www.ebi.ac.uk/pdbsum/4k2a PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k2a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k2a OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4k2a RCSB], [http://www.ebi.ac.uk/pdbsum/4k2a PDBsum]</span></td></tr> | ||
<table> | <table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The crystal structure of the novel haloalkane dehalogenase DbeA from Bradyrhizobium elkanii USDA94 revealed the presence of two chloride ions buried in the protein interior. The first halide-binding site is involved in substrate binding and is present in all structurally characterized haloalkane dehalogenases. The second halide-binding site is unique to DbeA. To elucidate the role of the second halide-binding site in enzyme functionality, a two-point mutant lacking this site was constructed and characterized. These substitutions resulted in a shift in the substrate-specificity class and were accompanied by a decrease in enzyme activity, stability and the elimination of substrate inhibition. The changes in enzyme catalytic activity were attributed to deceleration of the rate-limiting hydrolytic step mediated by the lower basicity of the catalytic histidine. | |||
Structural and functional analysis of a novel haloalkane dehalogenase with two halide-binding sites.,Chaloupkova R, Prudnikova T, Rezacova P, Prokop Z, Koudelakova T, Daniel L, Brezovsky J, Ikeda-Ohtsubo W, Sato Y, Kuty M, Nagata Y, Kuta Smatanova I, Damborsky J Acta Crystallogr D Biol Crystallogr. 2014 Jul;70(Pt 7):1884-97. doi:, 10.1107/S1399004714009018. Epub 2014 Jun 29. PMID:25004965<ref>PMID:25004965</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Dehalogenase|Dehalogenase]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
