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1 College of Pharmacy, Ewha Womans University, Seoul 120-750, Korea
2 Berkeley Structural Genomics Center, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA
3 Department of Chemistry, University of California, Berkeley, California 94720-5230, USA
(RECEIVED November 23, 2005; FINAL REVISION December 13, 2005; ACCEPTED December 13, 2005)
We have determined the crystal structure of the DUF16 domain of unknown function encoded by the gene MPN010 of Mycoplasma pneumoniae at 1.8 Å resolution. The crystal structure revealed that this domain is composed of two separated homotrimeric coiled-coils. The shorter one consists of 11 highly conserved residues. The sequence comprises noncanonical heptad repeats that induce a right-handed coiled-coil structure. The longer one is composed of approximately nine heptad repeats. In this coiledcoil structure, there are three distinguishable regions that confer unique structural properties compared with other known homotrimeric coiled-coils. The first part, containing one stutter, is an unusual phenylalanine-rich region that is not found in any other coiled-coil structures. The second part is a highly conserved glutamine-rich region, frequently found in other trimeric coiled-coil structures. The last part is composed of prototype heptad repeats. The phylogenetic analysis of the DUF16 family together with a secondary structure prediction shows that the DUF16 family can be classified into five subclasses according to N-terminal sequences. Based on the structural comparison with other coiledcoil structures, a probable molecular function of the DUF16 family is discussed.
Keywords: DUF16; MPN010; hypothetical protein; coiled-coil; stutter
Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051993506
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