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Protein Science, Vol 7, Issue 6 1477-1480, Copyright © 1998 by Cold Spring Harbor Laboratory Press
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A. BATEMAN, A. G. MURZIN and S. A. TEICHMANN
Medical Research Council Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, United Kingdom The Sanger Centre, Wellcome Trust Genome Campus, Hinxton, Cambridge, CB10 1SA, United Kingdom
We report the discovery of a novel family of proteins, each member contains tandem pentapeptide (five residue) repeats, described by the motif A(D/N)LXX. Members of this family are both membrane bound and cytoplasmic. The function of these repeats is uncertain, but they may have a targeting or structural function rather than enzymatic activity. This family is most common in cyanobacteria, suggesting a function related to cyanobacterial-specific metabolism. Although no experimental information is available for the structure of this family, it is predicted that the tandem pentapeptide repeats will form a right-handed {beta}-helical structure. A structural model of the pentapeptide repeats is presented.
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