3CJQ: Ribosomal Protein L11 Methyltransferase (Prma) In Complex With Dimethylated Ribosomal Protein L11 In Space Group P212121

Citation:
Abstract
Ribosomal protein L11 is a universally conserved component of the large subunit, and plays a significant role during initiation, elongation, and termination of protein synthesis. In Escherichia coli, the lysine methyltransferase PrmA trimethylates the N-terminal alpha-amino group and the epsilon-amino groups of Lys3 and Lys39. Here, we report four PrmA-L11 complex structures in different orientations with respect to the PrmA active site. Two structures capture the L11 N-terminal alpha-amino group in the active site in a trimethylated post-catalytic state and in a dimethylated state with bound S-adenosyl-L-homocysteine. Two other structures show L11 in a catalytic orientation to modify Lys39 and in a noncatalytic orientation. The comparison of complex structures in different orientations with a minimal substrate recognition complex shows that the binding mode remains conserved in all L11 orientations, and that substrate orientation is brought about by the unusual interdomain flexibility of PrmA.
PDB ID: 3CJQDownload
MMDB ID: 64573
PDB Deposition Date: 2008/3/13
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 3CJQ: dimeric; determined by author and by software (PISA)
Molecular Components in 3CJQ
Label Count Molecule
Proteins (2 molecules)
1
Ribosomal Protein L11 Methyltransferase(Gene symbol: prmA)
Molecule annotation
1
50S Ribosomal Protein L11
Molecule annotation
Chemicals (3 molecules)
1
1
2
1
3
1
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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