Crystal structure of Mil (Mth680)

Internal duplication and similarity between the Imp4/Brix domain and the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases

Chyan Leong Ng, David Waterman, Eugene V. Koonin, Alfred A. Antson, Miguel Ortiz-Lombardía

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Proteins of the Imp4/Brix superfamily are involved in ribosomal RNA processing, an essential function in all cells. We report the first structure of an Imp4/Brix superfamily protein, the Mil (for Methanothermobacter thermautotrophicus Imp4-like) protein (gene product Mth680), from the archaeon M. thermautotrophicus. The amino- and carboxy-terminal halves of Mil show significant structural similarity to one another, suggesting an origin by means of an ancestral duplication. Both halves show the same fold as the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases, with greater conservation seen in the N-terminal half. This structural similarity, together with the charge distribution in Mil, suggests that Imp4/Brix superfamily proteins could bind single-stranded segments of RNA along a concave surface formed by the N-terminal half of their β-sheet and a central α-helix. The crystal structure of Mil is incompatible with the presence, in the Imp4/ Brix domain, of a helix-turn-helix motif that was proposed to comprise the RNA-binding moiety of the Imp4/Brix proteins.

Original languageEnglish
Pages (from-to)140-146
Number of pages7
JournalEMBO Reports
Volume6
Issue number2
DOIs
Publication statusPublished - 2005
Externally publishedYes

Fingerprint

Methanobacteriaceae
Anticodon
Amino Acyl-tRNA Synthetases
Crystal structure
Proteins
Helix-Turn-Helix Motifs
RNA
Ribosomal RNA
Charge distribution
Archaea
Conservation
Processing

Keywords

  • Brix domain
  • Crystal structure
  • Imp4 domain
  • Methanothermobacter
  • RNA binding

ASJC Scopus subject areas

  • Genetics
  • Cell Biology

Cite this

Crystal structure of Mil (Mth680) : Internal duplication and similarity between the Imp4/Brix domain and the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases. / Ng, Chyan Leong; Waterman, David; Koonin, Eugene V.; Antson, Alfred A.; Ortiz-Lombardía, Miguel.

In: EMBO Reports, Vol. 6, No. 2, 2005, p. 140-146.

Research output: Contribution to journalArticle

@article{ac352d6550ed43ce9d1cc62f4924dc01,
title = "Crystal structure of Mil (Mth680): Internal duplication and similarity between the Imp4/Brix domain and the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases",
abstract = "Proteins of the Imp4/Brix superfamily are involved in ribosomal RNA processing, an essential function in all cells. We report the first structure of an Imp4/Brix superfamily protein, the Mil (for Methanothermobacter thermautotrophicus Imp4-like) protein (gene product Mth680), from the archaeon M. thermautotrophicus. The amino- and carboxy-terminal halves of Mil show significant structural similarity to one another, suggesting an origin by means of an ancestral duplication. Both halves show the same fold as the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases, with greater conservation seen in the N-terminal half. This structural similarity, together with the charge distribution in Mil, suggests that Imp4/Brix superfamily proteins could bind single-stranded segments of RNA along a concave surface formed by the N-terminal half of their β-sheet and a central α-helix. The crystal structure of Mil is incompatible with the presence, in the Imp4/ Brix domain, of a helix-turn-helix motif that was proposed to comprise the RNA-binding moiety of the Imp4/Brix proteins.",
keywords = "Brix domain, Crystal structure, Imp4 domain, Methanothermobacter, RNA binding",
author = "Ng, {Chyan Leong} and David Waterman and Koonin, {Eugene V.} and Antson, {Alfred A.} and Miguel Ortiz-Lombard{\'i}a",
year = "2005",
doi = "10.1038/sj.embor.7400328",
language = "English",
volume = "6",
pages = "140--146",
journal = "EMBO Reports",
issn = "1469-221X",
publisher = "Nature Publishing Group",
number = "2",

}

TY - JOUR

T1 - Crystal structure of Mil (Mth680)

T2 - Internal duplication and similarity between the Imp4/Brix domain and the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases

AU - Ng, Chyan Leong

AU - Waterman, David

AU - Koonin, Eugene V.

AU - Antson, Alfred A.

AU - Ortiz-Lombardía, Miguel

PY - 2005

Y1 - 2005

N2 - Proteins of the Imp4/Brix superfamily are involved in ribosomal RNA processing, an essential function in all cells. We report the first structure of an Imp4/Brix superfamily protein, the Mil (for Methanothermobacter thermautotrophicus Imp4-like) protein (gene product Mth680), from the archaeon M. thermautotrophicus. The amino- and carboxy-terminal halves of Mil show significant structural similarity to one another, suggesting an origin by means of an ancestral duplication. Both halves show the same fold as the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases, with greater conservation seen in the N-terminal half. This structural similarity, together with the charge distribution in Mil, suggests that Imp4/Brix superfamily proteins could bind single-stranded segments of RNA along a concave surface formed by the N-terminal half of their β-sheet and a central α-helix. The crystal structure of Mil is incompatible with the presence, in the Imp4/ Brix domain, of a helix-turn-helix motif that was proposed to comprise the RNA-binding moiety of the Imp4/Brix proteins.

AB - Proteins of the Imp4/Brix superfamily are involved in ribosomal RNA processing, an essential function in all cells. We report the first structure of an Imp4/Brix superfamily protein, the Mil (for Methanothermobacter thermautotrophicus Imp4-like) protein (gene product Mth680), from the archaeon M. thermautotrophicus. The amino- and carboxy-terminal halves of Mil show significant structural similarity to one another, suggesting an origin by means of an ancestral duplication. Both halves show the same fold as the anticodon-binding domain of class IIa aminoacyl-tRNA synthetases, with greater conservation seen in the N-terminal half. This structural similarity, together with the charge distribution in Mil, suggests that Imp4/Brix superfamily proteins could bind single-stranded segments of RNA along a concave surface formed by the N-terminal half of their β-sheet and a central α-helix. The crystal structure of Mil is incompatible with the presence, in the Imp4/ Brix domain, of a helix-turn-helix motif that was proposed to comprise the RNA-binding moiety of the Imp4/Brix proteins.

KW - Brix domain

KW - Crystal structure

KW - Imp4 domain

KW - Methanothermobacter

KW - RNA binding

UR - http://www.scopus.com/inward/record.url?scp=14644393728&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=14644393728&partnerID=8YFLogxK

U2 - 10.1038/sj.embor.7400328

DO - 10.1038/sj.embor.7400328

M3 - Article

VL - 6

SP - 140

EP - 146

JO - EMBO Reports

JF - EMBO Reports

SN - 1469-221X

IS - 2

ER -