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From Constructs to Crystals – Towards Structure Determination of β-barrel Outer Membrane Proteins
Published on: July 4, 2016
Crystal structure of the DUF16 domain of MPN010 from Mycoplasma pneumoniae
Dong Hae Shin1, Jeong-Sun Kim, Hisao Yokota
1College of Pharmacy, Ewha Womans Unversity, Seoul 120-750, Korea.
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 A 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.
Insights
Researchers determined the crystal structure of the DUF16 domain from Mycoplasma pneumoniae. This analysis revealed unique structural features of its homotrimeric coiled-coils, suggesting a probable molecular function for this unknown protein domain.
Area of Science:
- Structural Biology
- Mycoplasma pneumoniae research
- Protein domain analysis
Background:
- The DUF16 domain, encoded by MPN010 in Mycoplasma pneumoniae, is a domain of unknown function.
- Understanding the structure of such domains is crucial for elucidating their biological roles.
Purpose of the Study:
- To determine the high-resolution crystal structure of the DUF16 domain.
- To characterize the structural features of the DUF16 domain and compare them to known coiled-coil structures.
- To propose a probable molecular function for the DUF16 family based on structural and phylogenetic analyses.
Main Methods:
- X-ray crystallography to determine the crystal structure at 1.8 Å resolution.
- Sequence analysis and secondary structure prediction.
- Phylogenetic analysis of the DUF16 family.
Main Results:
- The crystal structure of the DUF16 domain revealed two distinct homotrimeric coiled-coils.
- The longer coiled-coil exhibits unique structural regions, including a phenylalanine-rich segment and a conserved glutamine-rich region.
- Phylogenetic analysis identified five subclasses within the DUF16 family based on N-terminal sequences.
Conclusions:
- The DUF16 domain possesses a unique homotrimeric coiled-coil structure with distinct regions.
- Structural insights provide a basis for inferring the probable molecular function of the DUF16 family.
- Further research can explore the functional implications of these structural findings in Mycoplasma pneumoniae.
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