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Crystal structure of a conserved hypothetical protein from Escherichia coli

  • Published:
Journal of Structural and Functional Genomics

Abstract

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 × 16 Å × 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.

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Authors and Affiliations

  1. Department of Chemistry, University of California, Berkeley, California, 94720-5230, USA

    Dong Hae Shin & Sung-Hou Kim

  2. Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California, 94720, USA

    Hisao Yokota, Rosalind Kim & Sung-Hou Kim

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  1. Dong Hae Shin
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  2. Hisao Yokota
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  4. Sung-Hou Kim
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Shin, D.H., Yokota, H., Kim, R. et al. Crystal structure of a conserved hypothetical protein from Escherichia coli . J Struct Func Genom 2, 53–66 (2002). https://doi.org/10.1023/A:1014450817696

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