 |
PDBsum entry 1ft8
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
RNA binding protein
|
PDB id
|
|
|
|
1ft8
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
242 a.a.
|
|
|
|
|
|
|
|
|
|
|
165 a.a.
|
|
|
|
|
|
|
|
|
|
|
44 a.a.
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
The structure of the mRNA export factor tap reveals a cis arrangement of a non-Canonical rnp domain and an lrr domain.
|
|
|
Authors
|
|
E.Liker,
E.Fernandez,
E.Izaurralde,
E.Conti.
|
|
|
Ref.
|
|
EMBO J, 2000,
19,
5587-5598.
[DOI no: ]
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
Human TAP is implicated in mRNA nuclear export and is used by simian type D
retroviruses to export their unspliced genomic RNA to the cytoplasm of the host
cell. We have determined the crystal structure of the minimal TAP fragment that
binds the constitutive transport element (CTE) of retroviral RNAs. Unexpectedly,
we find the fragment consists of a ribonucleoprotein (RNP) domain, which is not
identifiable by its sequence, and a leucine-rich repeat (LRR) domain. The
non-canonical RNP domain functions as the general RNA-binding portion of the
fragment. The LRR domain is required in cis to the RNP domain for CTE RNA
binding. The structural and biochemical properties of the domains point to a
remarkable similarity with the U2B"(RNP)-U2A'(LRR) spliceosomal
heterodimer. Our in vitro and in vivo functional studies using structure-based
mutants suggest that a phylogenetically conserved surface of the LRR domain of
TAP may have different roles in the export of viral and cellular RNAs.
|
|
|
|
|
|
|
|
Figure 1.
Figure 1 Domain structure of human TAP. The N-terminal region of
the molecule includes the minimal CTE RNA-binding fragment
(residues 102–372) (Braun et al., 1999). The domain boundaries
of the RNP and the LRR domains (shaded in gray) are as
identified from this work. The domain mapping of the C-terminal
region is as previously described (Bachi et al., 2000; Suyama et
al., 2000).
|
|
Figure 6.
Figure 6 Identification of putative macromolecular interaction
surfaces. (A) Ribbon diagram of the RNP domain in green with the
side chains of mutated residues in pink (see Figure 2C).
Residues that are essential for CTE binding are boxed. (B)
Surface representation of the RNP domain in a similar
orientation to (A). The surface is colored according to
electrostatic potential, with blue indicating positively charged
areas and red indicating negatively charged areas. (C) Structure
of the LRR domain viewed towards the convex  -helical
surface. Residues at this surface that have been mutated are
shown in pink (see Figure 3E). The molecule has been rotated
180° with respect to the view in Figure 3A. (D)
Electrostatic surface of the convex outer surface of the LRR
domain viewed as in (A), and colored as in (B). Residues whose
function is discussed in the text are labeled, and boxed when
essential.
|
|
|
|
|
|
The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(2000,
19,
5587-5598)
copyright 2000.
|
|
|
|
|
|
|
