Ontology highlight
ABSTRACT:
SUBMITTER: Fisher Z
PROVIDER: S-EPMC3371383 | biostudies-literature | 2011 Nov
REPOSITORIES: biostudies-literature
Fisher Zoë Z Kovalevsky Andrey Y AY Mustyakimov Marat M Silverman David N DN McKenna Robert R Langan Paul P
Biochemistry 20111012 44
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. ...[more]