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Crystal structure of the DUF16 domain of MPN010 from Mycoplasma pneumoniae

Title
Crystal structure of the DUF16 domain of MPN010 from Mycoplasma pneumoniae
Authors
Dong H.S.Kim J.-S.Yokota H.Kim R.Kim S.-H.
Ewha Authors
신동해
SCOPUS Author ID
신동해scopus
Issue Date
2006
Journal Title
Protein Science
ISSN
0961-8368JCR Link
Citation
vol. 15, no. 4, pp. 921 - 928
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
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 coiled-coil 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 coiled-coil structures, a probable molecular function of the DUF16 family is discussed. Copyright © 2006 The Protein Society.
DOI
10.1110/ps.051993506
Appears in Collections:
약학대학 > 약학과 > Journal papers
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