1DD3: Crystal Structure Of Ribosomal Protein L12 From Thermotoga Maritima

Citation:
Abstract
Protein L12, the only multicopy component of the ribosome, is presumed to be involved in the binding of translation factors, stimulating factor-dependent GTP hydrolysis. Crystal structures of L12 from Thermotogamaritima have been solved in two space groups by the multiple anomalous dispersion method and refined at 2.4 and 2.0 A resolution. In both crystal forms, an asymmetric unit comprises two full-length L12 molecules and two N-terminal L12 fragments that are associated in a specific, hetero-tetrameric complex with one non-crystallographic 2-fold axis. The two full-length proteins form a tight, symmetric, parallel dimer, mainly through their N-terminal domains. Each monomer of this central dimer additionally associates in a different way with an N-terminal L12 fragment. Both dimerization modes are unlike models proposed previously and suggest that similar complexes may occur in vivo and in situ. The structures also display different L12 monomer conformations, in accord with the suggested dynamic role of the protein in the ribosomal translocation process. The structures have been submitted to the Protein Databank (http://www.rcsb.org/pdb) under accession numbers 1DD3 and 1DD4.
PDB ID: 1DD3Download
MMDB ID: 14628
PDB Deposition Date: 1999/11/8
Updated in MMDB: 2016/12
Experimental Method:
x-ray diffraction
Resolution: 2  Å
Source Organism:
Similar Structures:
Biological Unit for 1DD3: trimeric; determined by author
Molecular Components in 1DD3
Label Count Molecule
Proteins (3 molecules)
2
50S Ribosomal Protein L7/l12(Gene symbol: rplL)
Molecule annotation
1
50S Ribosomal Protein L7/l12(Gene symbol: rplL)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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