Basic Tilted Helix Bundle – A new protein fold in human FKBP25/FKBP3 and HectD1

Journal Article · Fri Apr 25 00:00:00 EDT 2014 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/J.BBRC.2014.03.068· OSTI ID:22416397

Helander, Sara; Montecchio, Meri ^[1]; Lemak, Alexander ^[2]; Farès, Christophe ^[2]; Almlöf, Jonas ^[1]; Li, Yanjun ^[3]; Yee, Adelinda ^[2]; Arrowsmith, Cheryl H. ^[2]; Dhe-Paganon, Sirano ^[3]; Sunnerhagen, Maria ^[1]

---

1. Department of Physics, Chemistry and Biology, Division of Chemistry, Linköping University, SE-58183 Linköping (Sweden)
2. Princess Margaret Cancer Centre and Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 1L7 (Canada)
3. Structural Genomics Consortium, University of Toronto, 101 College St, Toronto, Ontario M5G 1L7 (Canada)

Highlights: • We describe the structure of a novel fold in FKBP25 and HectD. • The new fold is named the Basic Tilted Helix Bundle (BTHB) domain. • A conserved basic surface patch is presented, suggesting a functional role. - Abstract: In this paper, we describe the structure of a N-terminal domain motif in nuclear-localized FKBP25{sub 1–73}, a member of the FKBP family, together with the structure of a sequence-related subdomain of the E3 ubiquitin ligase HectD1 that we show belongs to the same fold. This motif adopts a compact 5-helix bundle which we name the Basic Tilted Helix Bundle (BTHB) domain. A positively charged surface patch, structurally centered around the tilted helix H4, is present in both FKBP25 and HectD1 and is conserved in both proteins, suggesting a conserved functional role. We provide detailed comparative analysis of the structures of the two proteins and their sequence similarities, and analysis of the interaction of the proposed FKBP25 binding protein YY1. We suggest that the basic motif in BTHB is involved in the observed DNA binding of FKBP25, and that the function of this domain can be affected by regulatory YY1 binding and/or interactions with adjacent domains.

• OSTI ID: 22416397
• Journal Information: Biochemical and Biophysical Research Communications, Vol. 447, Issue 1; Other Information: Copyright (c) 2014 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
DNA
HELA CELLS
HUMAN POPULATIONS
LIGASES
NUCLEAR MAGNETIC RESONANCE
PEPTIDES
SURFACES