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Biochem Biophys Res Commun. 2014 Apr 25;447(1):26-31. doi: 10.1016/j.bbrc.2014.03.068. Epub 2014 Mar 22.

Basic Tilted Helix Bundle - a new protein fold in human FKBP25/FKBP3 and HectD1.

Author information

1
Department of Physics, Chemistry and Biology, Division of Chemistry, Linköping University, SE-58183 Linköping, Sweden.
2
Northeast Structural Genomics Consortium and Ontario Cancer Institute, University Health Network, Toronto, Ontario, Canada.
3
Structural Genomics Consortium, Northeast Structural Genomics Consortium, Ontario, Canada.
4
Cancer Institute and Department of Medical Biophysics, University of Toronto, Ontario, Canada.
#
Contributed equally

Abstract

In this paper, we describe the structure of a N-terminal domain motif in nuclear-localized FKBP251-73, 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.

KEYWORDS:

FKBP25; FKBP3; HectD1; Immunophillins; NMR structure; Structural genomics; YY1

PMID:
24667607
PMCID:
PMC4116274
DOI:
10.1016/j.bbrc.2014.03.068
[Indexed for MEDLINE]
Free PMC Article

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