PDBsum entry: 1s79

RNA binding protein, translation

PDB id: 1s79

Contents

Protein chain

103 a.a. *

* Residue conservation analysis

PDB id:

1s79

Name:

RNA binding protein, translation

Title:

Solution structure of the central rrm of human la protein

Structure:

Lupus la protein. Chain: a. Fragment: central rrm. Synonym: sjogren syndrome type b antigen, ss-b, la ribonucleoprotein, la autoantigen. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: ssb. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

C.Alfano,D.Sanfelice,J.Babon,G.Kelly,A.Jacks,S.Curry, M.R.Conte

Key ref:

C.Alfano et al. (2004). Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein. Nat Struct Mol Biol, 11, 323-329. PubMed id: 15004549 DOI: 10.1038/nsmb747

Date:

29-Jan-04 Release date: 06-Apr-04

Protein chain

P05455  (LA_HUMAN) -  Lupus La protein

Seq: 408 a.a.

Struc: 103 a.a.*

* PDB and UniProt seqs differ at 5 residue positions (black crosses)

 Gene Ontology (GO) functional annotation 

• Cellular component: ribonucleoprotein complex (2 terms)
• Biological process: RNA processing (1 term)
• Biochemical function: nucleotide binding (3 terms)

DOI no: 10.1038/nsmb747

Nat Struct Mol Biol 11:323-329 (2004)

PubMed id: 15004549

Structural analysis of cooperative RNA binding by the La motif and central RRM domain of human La protein.

C.Alfano, D.Sanfelice, J.Babon, G.Kelly, A.Jacks, S.Curry, M.R.Conte.

ABSTRACT

The La protein is a conserved component of eukaryotic ribonucleoprotein complexes that binds the 3' poly(U)-rich elements of nascent RNA polymerase III (pol III) transcripts to assist folding and maturation. This specific recognition is mediated by the N-terminal domain (NTD) of La, which comprises a La motif and an RNA recognition motif (RRM). We have determined the solution structures of both domains and show that the La motif adopts an alpha/beta fold that comprises a winged-helix motif elaborated by the insertion of three helices. Chemical shift mapping experiments show that these insertions are involved in RNA interactions. They further delineate a distinct surface patch on each domain-containing both basic and aromatic residues-that interacts with RNA and accounts for the cooperative binding of short oligonucleotides exhibited by the La NTD.

Selected figure(s)

Figure 1.
Figure 1. Domain organization of human La and deletion mutants used in this study. Conventionally1, 2 human La is divided in two halves, N-terminal domain, comprising the La motif (domain 1) and the adjacent RRM (domain 2), and C-terminal domain, encompassing the RRM (domain 3), the SBM and the NLS (see text).

Figure 4.
Figure 4. Alignment of the La motif and central RRM sequences for La homologs.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Mol Biol (2004, 11, 323-329) copyright 2004.

Figures were selected by the author.