THE OCCUPANCY OF 2 DISTINCT CONFORMATIONS BY ACTIVE-SITE HISTIDINE-119 IN CRYSTALS OF RIBONUCLEASE IS MODULATED BY PH

被引：26

作者：

DEMEL, VSJ

DOSCHER, MS

MARTIN, PD

EDWARDS, BFP

机构：

[1] Department of Biochemistry, Wayne State University School of Medicine, Detroit, MI 48201

来源：

FEBS LETTERS | 1994年 / 349卷 / 01期

关键词：

MOBILE HISTIDINE; MODULATION OF CONFORMATION BY PH; PROTEIN SEMISYNTHESIS; RNASE MECHANISM OF ACTION; SEMISYNTHETIC RNASE; X-RAY STRUCTURE;

D O I：

10.1016/0014-5793(94)00664-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Structures of a semisynthetic RNase have been obtained to a resolution of 2.0 Angstrom at pH values of 5.2, 6.5, 7.5, and 8.8, respectively. The principle structural transformation occurring over this pH range is the conversion of the side chain of active site residue His-119 from one conformation (chi(1) = -43 degrees to -57 degrees) at low pH to another (chi(1) = +159 degrees to + 168 degrees) at higher pH values. On the basis of this observation, a model is proposed that reconciles the disparate pK values for His-119 in the enzyme-substrate complex that have been deduced from kinetic studies and from proton NMR measurements in the presence of pseudosubstrates.

引用

页码：155 / 160

页数：6

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