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1p3h

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(New page: 200px<br /><applet load="1p3h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p3h, resolution 2.8&Aring;" /> '''Crystal Structure of ...)
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Revision as of 21:19, 20 November 2007


1p3h, resolution 2.8Å

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Crystal Structure of the Mycobacterium tuberculosis chaperonin 10 tetradecamer

Overview

The crystal structure of Mycobacterium tuberculosis chaperonin 10, (cpn10(Mt)) has been determined to a resolution of 2.8 A. Two dome-shaped, cpn10(Mt) heptamers complex through loops at their bases to form a, tetradecamer with 72 symmetry and a spherical cage-like structure. The, hollow interior enclosed by the tetradecamer is lined with hydrophilic, residues and has dimensions of 30 A perpendicular to and 60 A along the, sevenfold axis. Tetradecameric cpn10(Mt) has also been observed in, solution by dynamic light scattering. Through its base loop sequence, cpn10(Mt) is known to be the agent in the bacterium responsible for bone, resorption and for the contribution towards its strong T-cell, immunogenicity. Superimposition of the cpn10(Mt) sequences 26 to 32 and 66, to 72 and E. coli GroES 25 to 31 associated with bone resorption activity, shows them to have similar conformations and structural features, suggesting that there may be a common receptor for the bone resorption, sequences. The base loops of cpn10s in general also attach to the, corresponding chaperonin 60 (cpn60) to enclose unfolded protein and to, facilitate its correct folding in vivo. Electron density corresponding to, a partially disordered protein subunit appears encapsulated within the, interior dome cavity of each heptamer. This suggests that the binding of, substrates to cpn10 is possible in the absence of cpn60.

About this Structure

1P3H is a Single protein structure of sequence from Mycobacterium tuberculosis with CA and MPD as ligands. This structure superseeds the now removed PDB entry 1JH2. Full crystallographic information is available from OCA.

Reference

Mycobacterium tuberculosis chaperonin 10 heptamers self-associate through their biologically active loops., Roberts MM, Coker AR, Fossati G, Mascagni P, Coates AR, Wood SP, J Bacteriol. 2003 Jul;185(14):4172-85. PMID:12837792

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