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Published online before print November 27, 2007, 10.1110/ps.073167408
Protein Science (2008), 17:154-158. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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PROTEIN STRUCTURE REPORT

The hypothetical protein Atu4866 from Agrobacterium tumefaciens adopts a streptavidin-like fold

Xuanjun Ai1,2, Anthony Semesi3, Adelinda Yee3, Cheryl H. Arrowsmith3, Wing-Yiu Choy1, and Shawn S.C. Li1,2

1 Department of Biochemistry, Schulich School of Medicine and Dentistry, The University of Western Ontario, London, Ontario N6A 5C1, Canada
2 Siebens-Drake Medical Research Institute, Schulich School of Medicine and Dentistry, The University of Western Ontario, London, Ontario N6A 5C1, Canada
3 Ontario Centre for Structural Proteomics, University Health Network, Toronto, Ontario M5G 2C4, Canada

(RECEIVED August 9, 2007; FINAL REVISION September 29, 2007; ACCEPTED October 1, 2007)

Atu4866 is a 79-residue conserved hypothetical protein of unknown function from Agrobacterium tumefaciens. Protein sequence alignments show that it shares ≥60% sequence identity with 20 other hypothetical proteins of bacterial origin. However, the structures and functions of these proteins remain unknown so far. To gain insight into the function of this family of proteins, we have determined the structure of Atu4866 as a target of a structural genomics project using solution NMR spectroscopy. Our results reveal that Atu4866 adopts a streptavidin-like fold featuring a β-barrel/sandwich formed by eight antiparallel β-strands. Further structural analysis identified a continuous patch of conserved residues on the surface of Atu4866 that may constitute a potential ligand-binding site.

Keywords: β-barrel; NMR; protein structure; structural genomics; streptavidin; Agrobacterium tumefaciens


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