PDBsum entry 1d7q

Gene regulation

PDB id: 1d7q

Contents

Protein chains

14 a.a.

143 a.a. *

* Residue conservation analysis

PDB id:

1d7q

Name:

Gene regulation

Title:

Human translation initiation factor eif1a

Structure:

Protein (n-terminal histidine tag). Chain: b. Engineered: yes. Translation initiation factor 1a. Chain: a. Engineered: yes

Source:

Synthetic: yes. Other_details: histidine tag is engineered into the vector that is expressed with the protein. Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

J.L.Battiste,T.V.Pestova,C.U.T.Hellen,G.Wagner

Key ref:

J.L.Battiste et al. (2000). The eIF1A solution structure reveals a large RNA-binding surface important for scanning function. Mol Cell, 5, 109-119. PubMed id: 10678173 DOI: 10.1016/S1097-2765(00)80407-4

Date:

19-Oct-99 Release date: 17-Mar-00

Protein chain

No UniProt id for this chain

Struc: 14 a.a.

Protein chain

P47813  (IF1AX_HUMAN) -  Eukaryotic translation initiation factor 1A, X-chromosomal from Homo sapiens

Seq: 144 a.a.

Struc: 143 a.a.

Enzyme reactions

• Enzyme class: Chain A: E.C.?

DOI no: 10.1016/S1097-2765(00)80407-4

Mol Cell 5:109-119 (2000)

PubMed id: 10678173

The eIF1A solution structure reveals a large RNA-binding surface important for scanning function.

J.L.Battiste, T.V.Pestova, C.U.Hellen, G.Wagner.

ABSTRACT

The translation initiation factor eIF1A is necessary for directing the 43S preinitiation complex from the 5' end of the mRNA to the initiation codon in a process termed scanning. We have determined the solution structure of human eIF1A, which reveals an oligonucleotide-binding (OB) fold and an additional domain. NMR titration experiments showed that eIF1A binds single-stranded RNA oligonucleotides in a site-specific, but non-sequence-specific manner, hinting at an mRNA interaction rather than specific rRNA or tRNA binding. The RNA binding surface extends over a large area covering the canonical OB fold binding site as well as a groove leading to the second domain. Site-directed mutations at multiple positions along the RNA-binding surface were defective in the ability to properly assemble preinitiation complexes at the AUG codon in vitro.

Selected figure(s)

Figure 1.
Figure 1. Sequence Homology of eIF1A-like Proteins across All KingdomsSequence alignments adapted from the paper by [25]. Amino acids that have greater than 50% identity over 12 sequences analyzed by Kyrpides (more than shown in figure) are shaded. Identities between human and yeast are shown with black circles (65% identity). Side bars indicate sequences from eukaryotes (E), archaebacteria (A), and eubacteria (B/IF1). The secondary structure of human eIF1A (determined in this paper) over the region that has observable long-range NOEs is shown below the sequence (wavy lines indicate coils or turns; arrows indicate strands; cylinders indicate helices). The secondary structure elements are labeled β for β strand, α for α and 3[10] helices, L for loops connecting β strands or helices, N for amino-terminal strand, C for carboxy-terminal strand. Loop numbering indicates the secondary structure elements connect by the loops (adapted from [32]). For instance, L12 connects strand 1 and 2, and L3α connects strand 3 and the subsequent helix 1. Organisms are: HUMAN, Homo sapiens; YEAST, Saccharomyces cerevisiae; METJA, Methanococcus jannaschii; ARCFU, Archaeoglobus fulgidus; ECOLI, Escherichia coli; BACSU, Bacillus subtilis.

Figure 5.
Figure 5. Molecular Surfaces of eIF1A(A) Three views of the electrostatic surface of eIF1A produced with the program GRASP ([33]). Positive charge is colored blue and negative red (±40 kT). Surfaces to the right are progressively rotated 90° counterclockwise around the vertical axis of the paper. eIF1A is in a different orientation from the other figures with the far right panel looking down the axis/hole of the β barrel (approximately 90° clockwise rotation of Figure 4B around horizontal axis of paper). Secondary structure elements are labeled for orientation.(B) Surface of amino acids that have backbone amide chemical shift changes upon binding RNA are colored green (same residues as Figure 4B). Yellow surfaces are amino acids that have undetectable amide resonances due to intermediate conformational exchange in the unbound protein and are not available as probes of RNA binding. The three surfaces have the same orientation as in (A).

The above figures are reprinted by permission from Cell Press: Mol Cell (2000, 5, 109-119) copyright 2000.

Figures were selected by an automated process.