Structural properties of human carbonic anhydrase II at pH 9.5.

Abstract:

:The structure of human carbonic anhydrase II at pH 9.5 has been studied by X-ray crystallographic methods to 2.2 A 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 chi 1. 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.

authors

Nair SK,Christianson DW

doi

10.1016/0006-291x(91)91229-6

subject

Has Abstract

pub_date

1991-12-16 00:00:00

pages

579-84

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(91)91229-6

journal_volume

181

pub_type

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