4KB2

Crystal structure of ribosome recycling factor mutant R109A from Mycobacterium tuberculosis

Summary for 4KB2

• Entry DOI: 10.2210/pdb4kb2/pdb
• Related: 1WQF 1WQG 1WQH 4KAW 4KB4 4KC6 4KDD
• Descriptor: Ribosome-recycling factor, CADMIUM ION (3 entities in total)
• Functional Keywords: ribosome recycling factor, ribosomes, translation, eubacteria, post-termination complex, elongation factor g, bacterial cytosol
• Biological source: Mycobacterium tuberculosis
• Total number of polymer chains: 1
• Total formula weight: 21112.78

Authors

Selvaraj, M.,Govindan, A.,Seshadri, A.,Dubey, B.,Varshney, U.,Vijayan, M. (deposition date: 2013-04-23, release date: 2014-03-12, Last modification date: 2023-11-08)

Primary citation

Selvaraj, M.,Govindan, A.,Seshadri, A.,Dubey, B.,Varshney, U.,Vijayan, M.
Molecular flexibility of Mycobacterium tuberculosis ribosome recycling factor and its functional consequences: an exploration involving mutants.
J.Biosci., 38:845-855, 2013

PubMed Abstract: Internal mobility of the two domain molecule of ribosome recycling factor (RRF) is known to be important for its action. Mycobacterium tuberculosis RRF does not complement E. coli for its deficiency of RRF (in the presence of E. coli EF-G alone). Crystal structure had revealed higher rigidity of the M. tuberculosis RRF due to the presence of additional salt bridges between domains. Two inter-domain salt bridges and one between the linker region and the domain containing C-terminal residues were disrupted by appropriate mutations. Except for a C-terminal deletion mutant, all mutants showed RRF activity in E. coli when M. tuberculosis EF-G was also co-expressed. The crystal structures of the point mutants, that of the C-terminal deletion mutant and that of the protein grown in the presence of a detergent, were determined. The increased mobility resulting from the disruption of the salt bridge involving the hinge region allows the appropriate mutant to weakly complement E. coli for its deficiency of RRF even in the absence of simultaneous expression of the mycobacterial EF-G. The loss of activity of the C-terminal deletion mutant appears to be partly due to the rigidification of the molecule consequent to changes in the hinge region.

PubMed: 24296887
DOI: 10.1007/s12038-013-9381-0

Experimental method

X-RAY DIFFRACTION (2.3 Å)