PDBsum entry 2mtf

RNA binding protein

PDB id: 2mtf

Contents

Protein chain

114 a.a.

PDB id:

2mtf

Name:

RNA binding protein

Title:

Solution structure of the la motif of human larp6

Structure:

La-related protein 6. Chain: a. Synonym: acheron, achn, la ribonucleoprotein domain family member 6. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: larp6. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

L.Martino,N.Jh.Salisbury,A.R.Atkinson,G.Kelly,M.R.Conte

Key ref:

L.Martino et al. (2015). Synergic interplay of the La motif, RRM1 and the interdomain linker of LARP6 in the recognition of collagen mRNA expands the RNA binding repertoire of the La module. Nucleic Acids Res, 43, 645-660. PubMed id: 25488812 DOI: 10.1093/nar/gku1287

Date:

18-Aug-14 Release date: 24-Dec-14

Protein chain

Q9BRS8  (LARP6_HUMAN) -  La-related protein 6 from Homo sapiens

Seq: 491 a.a.

Struc: 114 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1093/nar/gku1287

Nucleic Acids Res 43:645-660 (2015)

PubMed id: 25488812

Synergic interplay of the La motif, RRM1 and the interdomain linker of LARP6 in the recognition of collagen mRNA expands the RNA binding repertoire of the La module.

L.Martino, S.Pennell, G.Kelly, B.Busi, P.Brown, R.A.Atkinson, N.J.Salisbury, Z.H.Ooi, K.W.See, S.J.Smerdon, C.Alfano, T.T.Bui, M.R.Conte.

ABSTRACT

The La-related proteins (LARPs) form a diverse group of RNA-binding proteins characterized by the possession of a composite RNA binding unit, the La module. The La module comprises two domains, the La motif (LaM) and the RRM1, which together recognize and bind to a wide array of RNA substrates. Structural information regarding the La module is at present restricted to the prototypic La protein, which acts as an RNA chaperone binding to 3' UUUOH sequences of nascent RNA polymerase III transcripts. In contrast, LARP6 is implicated in the regulation of collagen synthesis and interacts with a specific stem-loop within the 5' UTR of the collagen mRNA. Here, we present the structure of the LaM and RRM1 of human LARP6 uncovering in both cases considerable structural variation in comparison to the equivalent domains in La and revealing an unprecedented fold for the RRM1. A mutagenic study guided by the structures revealed that RNA recognition requires synergy between the LaM and RRM1 as well as the participation of the interdomain linker, probably in realizing tandem domain configurations and dynamics required for substrate selectivity. Our study highlights a considerable complexity and plasticity in the architecture of the La module within LARPs.