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Crystallization and preliminary X-ray crystallographic analysis of an artificial molten-globular-like triosephosphate isomerase protein of mixed phylogenetic origin

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Title Crystallization and preliminary X-ray crystallographic analysis of an artificial molten-globular-like triosephosphate isomerase protein of mixed phylogenetic origin
 
Creator GOYAL, VD
YADAV, P
KUMAR, A
GHOSH, B
MAKDE, RD
 
Subject SEQUENCE STATISTICS
TPR MOTIF
CONSENSUS
DESIGN
CRYSTALS
FOLD
TIM
 
Description A bioinformatics-based protein-engineering approach called consensus design led to the construction of a chimeric triosephosphate isomerase (TIM) protein called ccTIM (curated consensus TIM) which is as active as Saccharomyces cerevisiae TIM despite sharing only 58% sequence identity with it. The amino-acid sequence of this novel protein is as identical to native sequences from eukaryotes as to those from prokaryotes and shares some biophysical traits with a molten globular protein. Solving its crystal structure would help in understanding the physical implications of its bioinformatics-based sequence. In this report, the ccTIM protein was successfully crystallized using the microbatch-under-oil method and a full X-ray diffraction data set was collected to 2.2 angstrom resolution using a synchrotron-radiation source. The crystals belonged to space group C222(1), with unit-cell parameters a = 107.97, b = 187.21, c = 288.22 angstrom. Matthews coefficient calculations indicated the presence of six dimers in the asymmetric unit, with an approximate solvent content of 46.2%.
 
Publisher WILEY-BLACKWELL
 
Date 2014-12-29T06:19:12Z
2014-12-29T06:19:12Z
2014
 
Type Article
 
Identifier ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, 701521-1525
1744-3091
http://dx.doi.org/10.1107/S2053230X14020755
http://dspace.library.iitb.ac.in/jspui/handle/100/17293
 
Language English