Structural properties of human carbonic anhydrase II at pH 9.5

Satish K. Nair, David W. Christianson

Research output: Contribution to journalArticlepeer-review

Abstract

The structure of human carbonic anhydrase II at pH 9.5 has been studied by X-ray crystallographic methods to 2.2 Å resolution. These studies complement those performed under acidic conditions in which the catalytically-important proton-shuttle group, His-64, exhibits conformational mobility about side-chain torsion angle χ1. However, no structural changes are observed in the conformation of His-64 at high pH. Therefore, we conclude that the protonation of His-64 (as well as zinc-bound hydroxide) may be a factor which contributes to the predominantly "out" conformation for His-64 observed at low pH.

Original languageEnglish (US)
Pages (from-to)579-584
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume181
Issue number2
DOIs
StatePublished - Dec 16 1991
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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