PDBsum entry: 1dm9

Structural genomics

PDB id: 1dm9

Contents

Protein chains

104 a.a. *

Ligands

SO4 ×6

Waters ×141

* Residue conservation analysis

PDB id:

1dm9

Name:

Structural genomics

Title:

Heat shock protein 15 kd

Structure:

Hypothetical 15.5 kd protein in mrca-pcka intergenic region. Chain: a, b

Source:

Escherichia coli. Organism_taxid: 562

Biol. unit:

Tetramer (from PQS)

Resolution:

2.00Å R-factor: 0.226 R-free: 0.286

Authors:

B.L.Staker,P.Korber,J.C.A.Bardwell,M.A.Saper

Key ref:

B.L.Staker et al. (2000). Structure of Hsp15 reveals a novel RNA-binding motif. EMBO J, 19, 749-757. PubMed id: 10675344 DOI: 10.1093/emboj/19.4.749

Date:

14-Dec-99 Release date: 18-Feb-00

Protein chains

P0ACG8  (HSLR_ECOLI) -  Heat shock protein 15

Seq: 133 a.a.

Struc: 104 a.a.

 Gene Ontology (GO) functional annotation 

• Biological process: response to stress (3 terms)
• Biochemical function: protein binding (5 terms)

DOI no: 10.1093/emboj/19.4.749

EMBO J 19:749-757 (2000)

PubMed id: 10675344

Structure of Hsp15 reveals a novel RNA-binding motif.

B.L.Staker, P.Korber, J.C.Bardwell, M.A.Saper.

ABSTRACT

We have solved the crystal structure of the heat shock protein Hsp15, a newly isolated and very highly inducible heat shock protein that binds the ribosome. Comparison of its structure with those of two RNA-binding proteins, ribosomal protein S4 and threonyl-tRNA synthetase, reveals a novel RNA-binding motif. This newly recognized motif is remarkably common, present in at least eight different protein families that bind RNA. The motif's surface is populated by conserved, charged residues that define a likely RNA-binding site. An intriguing pattern emerges: stress proteins, ribosomal proteins and tRNA synthetases repeatedly share a conserved motif. This may imply a hitherto unrecognized functional similarity between these three protein classes.

Selected figure(s)

Figure 1.
Figure 1 Ribbon representation of Hsp15 colored by conservation. (A) Forty-three eubacterial members of the Hsp15 family were identified by a BLAST search of the non-redundant database and the unfinished microbial databases in July, 1999 (Altschul et al., 1997). Green residues are identical or contain conservative substitutions in at least 50% of the sequences. Residues 4–110 are shown. The portion of the L loop is labeled with an L. (B) As (A), but oriented with the proposed RNA-binding L motif in front. This is the orientation of Hsp15 used in all subsequent figures.

Figure 5.
Figure 5 The L motif in three different protein structures. The peptide backbones of three structures, ribosomal protein S4, Hsp15 and threonyl-tRNA, are compared. The region highlighted in color is the L motif that is shared by all three proteins. (A) Hsp15 with its L motif highlighted in yellow. (B) Ribosomal protein S4 with its L motif highlighted in blue. (C) Threonyl-tRNA synthetase with its L motif highlighted in red. (D) Overlay of residues 9–57 of Hsp15 (yellow), 92–141 of ribosomal protein S4 (blue) and 18–59 of threonyl-tRNA synthetase (red).

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (2000, 19, 749-757) copyright 2000.

Figures were selected by the author.