1IQV

Crystal Structure Analysis of the archaebacterial ribosomal protein S7

Summary for 1IQV

• Entry DOI: 10.2210/pdb1iqv/pdb
• Descriptor: RIBOSOMAL PROTEIN S7 (2 entities in total)
• Functional Keywords: ribosomal protein, rna-binding, decoding center, helix-turn-helix, ribosome
• Biological source: Pyrococcus horikoshii
• Total number of polymer chains: 1
• Total formula weight: 25029.23

Authors

Hosaka, H.,Yao, M.,Kimura, M.,Tanaka, I. (deposition date: 2001-08-07, release date: 2001-08-29, Last modification date: 2023-10-25)

Primary citation

Hosaka, H.,Yao, M.,Kimura, M.,Tanaka, I.
The structure of the archaebacterial ribosomal protein S7 and its possible interaction with 16S rRNA.
J.Biochem., 130:695-701, 2001

PubMed Abstract: Ribosomal protein S7 is one of the ubiquitous components of the small subunit of the ribosome. It is a 16S rRNA-binding protein positioned close to the exit of the tRNA, and it plays a role in initiating assembly of the head of the 30S subunit. Previous structural analyses of eubacterial S7 have shown that it has a stable alpha-helix core and a flexible beta-arm. Unlike these eubacterial proteins, archaebacterial or eukaryotic S7 has an N-terminal extension of approximately 60 residues. The crystal structure of S7 from archaebacterium Pyrococcus horikoshii (PhoS7) has been determined at 2.1 A resolution. The final model of PhoS7 consists of six major alpha-helices, a short 3(10)-helix and two beta-stands. The major part (residues 18-45) of the N-terminal extension of PhoS7 reinforces the alpha-helical core by well-extended hydrophobic interactions, while the other part (residues 46-63) is not visible in the crystal and is possibly fixed only by interacting with 16S rRNA. These differences in the N-terminal extension as well as in the insertion (between alpha1 and alpha2) of the archaebacterial S7 structure from eubacterial S7 are such that they do not necessitate a major change in the structure of the currently available eubacterial 16S rRNA. Some of the inserted chains might pass through gaps formed by helices of the 16S rRNA.

PubMed: 11686933
DOI: 10.1093/oxfordjournals.jbchem.a003036

Experimental method

X-RAY DIFFRACTION (2.1 Å)