PDBsum entry 1v8q

Translation

PDB id: 1v8q

Contents

Protein chains

66 a.a. *

Ligands

DTT

Waters ×18

* Residue conservation analysis

PDB id:

1v8q

Name:

Translation

Title:

Crystal structure of ribosomal protein l27 from thermus thermophilus hb8

Structure:

Tt0826. Chain: a, b, c, d. Engineered: yes

Source:

Thermus thermophilus. Organism_taxid: 274. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.80Å R-factor: 0.197 R-free: 0.236

Authors:

H.Wang,C.Takemoto-Hori,K.Murayama,T.Terada,M.Shirouzu,S.Kuramitsu, S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)

Key ref:

H.Wang et al. (2004). Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8. Protein Sci, 13, 2806-2810. PubMed id: 15340170 DOI: 10.1110/ps.04864904

Date:

13-Jan-04 Release date: 13-Jul-04

Protein chains

P60493  (RL27_THET8) -  Large ribosomal subunit protein bL27 from Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

Seq: 85 a.a.

Struc: 66 a.a.

DOI no: 10.1110/ps.04864904

Protein Sci 13:2806-2810 (2004)

PubMed id: 15340170

Crystal structure of ribosomal protein L27 from Thermus thermophilus HB8.

H.Wang, C.H.Takemoto, K.Murayama, H.Sakai, A.Tatsuguchi, T.Terada, M.Shirouzu, S.Kuramitsu, S.Yokoyama.

ABSTRACT

Ribosomal protein L27 is located near the peptidyltransferase center at the interface of ribosomal subunits, and is important for ribosomal assembly and function. We report the crystal structure of ribosomal protein L27 from Thermus thermophilus HB8, which was determined by the multiwavelength anomalous dispersion method and refined to an R-factor of 19.7% (R(free) = 23.6%) at 2.8 A resolution. The overall fold is an all beta-sheet hybrid. It consists of two sets of four-stranded beta-sheets formed around a well-defined hydrophobic core, with a highly positive charge on the protein surface. The structure of ribosomal protein L27 from T. thermophilus HB8 in the RNA-free form is investigated, and its functional roles in the ribosomal subunit are discussed.

Selected figure(s)

Figure 1.
Figure 1. (A) Alignment of the ribosomal protein L27 sequences from T. thermophilus HB8, D. radiodurans, and E. coli. The multiple alignment was achieved with CLUSTAL X (Thompson et al. 1997). The secondary structural elements, determined on the basis of the X-ray structure of T. thermophilus protein L27, are indicated with arrows for -strands and a coil for a 3[10] helix at the top of the alignment. The identical amino acid residues are shown in white letters highlighted in red, whereas the similar residues are shown in red letters. (B) Stereo structure of the T. thermophilus protein L27. The stereo views were prepared by the programs MOLSCRIPT (Kraulis et al. 1991) and RASTER3D (Merritt and Bacon 1997). (C) Electrostatic potential surface of the T. thermophilus ribosomal protein L27. The molecular surface presentation was generated by GRASP (Nicholls et al. 1991).

The above figure is reprinted by permission from the Protein Society: Protein Sci (2004, 13, 2806-2810) copyright 2004.

Figure was selected by an automated process.