Crystal structure of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26 at 0.95 A resolution: dynamics of catalytic residues.

@article{Oakley2004CrystalSO,
  title={Crystal structure of haloalkane dehalogenase LinB from Sphingomonas paucimobilis UT26 at 0.95 A resolution: dynamics of catalytic residues.},
  author={Aaron J Oakley and Martin Klvaňa and Michal Otyepka and Yuji Nagata and Matthew C. J. Wilce and Jir{\'i} Damborsk{\'y}},
  journal={Biochemistry},
  year={2004},
  volume={43 4},
  pages={
          870-8
        }
}
We present the structure of LinB, a 33-kDa haloalkane dehalogenase from Sphingomonas paucimobilis UT26, at 0.95 A resolution. The data have allowed us to directly observe the anisotropic motions of the catalytic residues. In particular, the side-chain of the catalytic nucleophile, Asp108, displays a high degree of disorder. It has been modeled in two conformations, one similar to that observed previously (conformation A) and one strained (conformation B) that approached the catalytic base… CONTINUE READING
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