Abstract
A phosphoribosyl anthranilate isomerase,TkTrpF, fromThermococcus kodakaraensiswas expressed inEscherichia coliand purified to homogeneity.TkTrpF was crystallized and its structure was determined by molecular replacement in two different space groups (C2 andP1) using data to 1.85 and 1.75 Å resolution, respectively.TkTrpF belongs to the class of TIM-barrel proteins. Structural comparison with other phosphoribosyl anthranilate isomerases (TrpFs) showed the highest structural similarity toPyrococcus furiosusTrpF. Similarly toP. furiosusTrpF,TkTrpF is a monomer in solution, in contrast to other thermophilic enzymes, which exist as functional dimers. Although in space groupP1TkTrpF crystallizes with two molecules in the asymmetric unit, the interface is highly improbable in solution. Potential factors for the thermostability ofTkTrpF were attributed to an increase in helical structure, an increased number of charged residues and an increase in the number of salt bridges.
Publisher
International Union of Crystallography (IUCr)
Subject
Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics
Cited by
3 articles.
订阅此论文施引文献
订阅此论文施引文献,注册后可以免费订阅5篇论文的施引文献,订阅后可以查看论文全部施引文献