title: Neutron structure of human carbonic anhydrase II: a hydrogen-bonded water network "switch" is observed between pH 7.8 and 10.0.
abstract: The neutron structure of wild-type human carbonic anhydrase II at pH 7.8 has been determined to 2.0 Å resolution. Detailed analysis and comparison to the previously determined structure at pH 10.0 show important differences in the protonation of key catalytic residues in the active site as well as a rearrangement of the H-bonded water network. For the first time, a completed H-bonded network stretching from the Zn-bound solvent to the proton shuttling residue, His64, has been directly observed.
authors: Bioscience Division, Los Alamos National Laboratory, Los Alamos, New Mexico 87544, United States. zfisher@lanl.gov
authors: Zoë
authors: Z
authors: Fisher
authors: Andrey Y
authors: AY
authors: Kovalevsky
authors: Marat
authors: M
authors: Mustyakimov
authors: David N
authors: DN
authors: Silverman
authors: Robert
authors: R
authors: McKenna
authors: Paul
authors: P
authors: Langan
mesh_terms: D024402:Carbonic Anhydrase II / Q000737:chemistry* / Q000378:metabolism; D020134:Catalytic Domain; D018360:Crystallography, X-Ray; D006801:Humans; D006860:Hydrogen Bonding; D006863:Hydrogen-Ion Concentration; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism; D009501:Neutron Activation Analysis / Q000379:methods; D011522:Protons; D012996:Solutions; D014867:Water / Q000737:chemistry* / Q000378:metabolism
chemical_list: D007527:Isoenzymes; D011522:Protons; D012996:Solutions; D014867:Water; D024402:Carbonic Anhydrase II