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The hypothetical protein Atu4866 from Agrobacterium tumefaciens adopts a streptavidin‐like fold
Author(s) -
Ai Xuanjun,
Semesi Anthony,
Yee Adelinda,
Arrowsmith Cheryl H.,
Choy WingYiu,
Li Shawn S.C.
Publication year - 2008
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.073167408
Subject(s) - agrobacterium tumefaciens , streptavidin , fold (higher order function) , computational biology , microbiology and biotechnology , chemistry , biology , biochemistry , computer science , transformation (genetics) , programming language , biotin , gene
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.