PORPHOBILINOGEN DEAMINASE AND ITS STRUCTURAL SIMILARITY TO THE BIDOMAIN BINDING-PROTEINS

被引：24
|
作者：
LOUIE, GV
机构：
[1] Laboratory of Molecular Biology, Department of Crystallography, Birkbeck College, London, WC1E 7HX, Malet Street
来源：
CURRENT OPINION IN STRUCTURAL BIOLOGY | 1993年 / 3卷 / 03期
基金：
英国医学研究理事会;
关键词：
D O I：
10.1016/S0959-440X(05)80113-7
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：
The tetrapyrrole-biosynthesis enzyme porphobilinogen deaminase has in two of its domains the same alpha/beta polypeptide-chain fold as the transferrins and the periplasmic binding proteins. These proteins have in common an active-site cleft located at the interface between two domains. The binding proteins and porphobilinogen deaminase are likely related by divergent evolution. The interdomain motions observed in the binding proteins are suggested also to have an important role in the mechanism of the reaction catalyzed by porphobilinogen deaminase.
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页码：401 / 408
页数：8
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