Journal of Structural and Functional Genomics
Online ISSN : 1345-711X
ISSN-L : 1345-711X
Crystal structure of a conserved hypothetical protein from Escherichia coli
Dong Hae ShinHisao YokotaRosalind KimSung-Hou Kim
Author information

2001 Volume 2-pre Issue 1 Pages L149-L186


The crystal structure of a conserved hypothetical protein from Escherichia coli has been determined using X-ray crystallography. The protein belongs to the Cluster of Orthologous Group COG1553 (National Center for Biotechnology Information database, NLM, NIH), for which there was no structural information available until now. Structural homology search with DALI algorism indicated that this protein has a new fold with no obvious similarity to those of other proteins with known three-dimensional structures. The protein quaternary structure consists of a dimer of trimers, which makes a characteristic cylinder shape. There is a large closed cavity with approximate dimensions of 16 Å x 16 Å x 20 Å in the center of the hexameric structure. Six putative active sites are positioned along the equatorial surface of the hexamer. There are several highly conserved residues including two possible functional cysteines in the putative active site. The possible molecular function of the protein is discussed.

Information related to the author

This article cannot obtain the latest cited-by information.

© 2001 Kluwer Academic Publishers
Previous article