1kd1

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spinqualitylabelsall models 1kd1, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Co-crystal Structure of Spiramycin bound to the 50S Ribosomal Subunit of Haloarcula marismortui

Overview

Crystal structures of the Haloarcula marismortui large ribosomal subunit, complexed with the 16-membered macrolide antibiotics carbomycin A, spiramycin, and tylosin and a 15-membered macrolide, azithromycin, show, that they bind in the polypeptide exit tunnel adjacent to the peptidyl, transferase center. Their location suggests that they inhibit protein, synthesis by blocking the egress of nascent polypeptides. The saccharide, branch attached to C5 of the lactone rings extends toward the peptidyl, transferase center, and the isobutyrate extension of the carbomycin A, disaccharide overlaps the A-site. Unexpectedly, a reversible covalent bond, forms between the ethylaldehyde substituent at the C6 position of the, 16-membered macrolides and the N6 of A2103 (A2062, E. coli). Mutations in, 23S rRNA that result in clinical resistance render the binding site less, complementary to macrolides.

About this Structure

1KD1 is a Protein complex structure of sequences from Haloarcula marismortui with SPR, MG, NA, CD, CL and K as ligands. Full crystallographic information is available from OCA.

Reference

The structures of four macrolide antibiotics bound to the large ribosomal subunit., Hansen JL, Ippolito JA, Ban N, Nissen P, Moore PB, Steitz TA, Mol Cell. 2002 Jul;10(1):117-28. PMID:12150912

Page seeded by OCA on Tue Nov 20 19:04:19 2007