TY - JOUR
T1 - Structural properties of human carbonic anhydrase II at pH 9.5
AU - Nair, Satish K.
AU - Christianson, David W.
N1 - Funding Information:
We thank the NSF for grant DIR-8821184 (i n support of the X-ray data acquisition equipment) and the NIH for grant GM45614. Additionally, D.W.C. is grateful to the Office of Naval Researchf or a Young Investigator Award. S.K.N. is supported by N.I.H. Training Grant GM07229.
PY - 1991/12/16
Y1 - 1991/12/16
N2 - 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.
AB - 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.
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U2 - 10.1016/0006-291X(91)91229-6
DO - 10.1016/0006-291X(91)91229-6
M3 - Article
C2 - 1755840
AN - SCOPUS:0026351203
VL - 181
SP - 579
EP - 584
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -