Crystal structure analysis of a hypothetical protein (MJ0366) from Methanocaldococcus jannaschii revealed a novel topological arrangement of the knot fold

Journal Article · Sat Jan 07 23:00:00 EST 2017 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/J.BBRC.2016.11.052· OSTI ID:22696752

Thiruselvam, Viswanathan ^[1]; Kumarevel, Thirumananseri ^[2]; Karthe, Ponnuraj ^[1]; Kuramitsu, Seiki ^[3]; Yokoyama, Shigeyuki ^[2]

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1. Centre of Advanced Study in Crystallography and Biophysics, University of Madras, Guindy Campus, Chennai, 600025 (India)
2. RIKEN Structural Biology Laboratory, Yokohama Institute, RIKEN, 1-7-22 Suehiro-cho, Tsurumi, Yokohama, 230-0045 (Japan)
3. Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka, 560-0043 (Japan)

The crystal structure of a hypothetical protein MJ0366, derived from Methanocaldococcus jannaschii was solved at 1.9 Å resolution using synchrotron radiation. MJ0366 was crystallized as a monomer and has knot structural arrangement. Intriguingly, the solved structure consists of novel ‘KNOT’ fold conformation. The 3{sub 1} trefoil knot was observed in the structure. The N-terminal and C-terminal ends did not participate in knot formation. - Highlights: • Crystal structure of a hypothetical protein from Methanocaldococcus jannaschii was determined. • The protein adopts novel knot fold conformation. • Structure of the first smallest knot protein was solved.

• OSTI ID: 22696752
• Journal Information: Biochemical and Biophysical Research Communications, Journal Name: Biochemical and Biophysical Research Communications Journal Issue: 2 Vol. 482; ISSN 0006-291X; ISSN BBRCA9
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
CRYSTAL STRUCTURE
CRYSTALS
MONOMERS
PROTEINS
RESOLUTION
SYNCHROTRON RADIATION
SYNCHROTRONS
TOPOLOGY