4k2a
From Proteopedia
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<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. | ||
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| + | 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> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
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| + | ==See Also== | ||
| + | *[[Dehalogenase|Dehalogenase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 05:49, 24 September 2014
Crystal structure of haloalkane dehalogenase DbeA from Bradyrhizobium elkani USDA94
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Categories: Haloalkane dehalogenase | Chaloupkova, R. | Damborsky, J. | Koudelakova, T. | Kuty, M. | Mozga, T. | Nagata, Y. | Prudnikova, T. | Rezacova, P. | S2F, Structure 2.Function Project. | Sato, Y. | Smatanova, I Kuta. | Dimer catalytic pentad | Enzyme function initiative | Halogen binding | Hydrolase | S2f | Structural genomic | Structure 2 function project | Two domain organization
