1iok
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(New page: 200px<br /><applet load="1iok" size="450" color="white" frame="true" align="right" spinBox="true" caption="1iok, resolution 3.20Å" /> '''CRYSTAL STRUCTURE OF...)
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Revision as of 15:25, 20 November 2007
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CRYSTAL STRUCTURE OF CHAPERONIN-60 FROM PARACOCCUS DENITRIFICANS
Overview
The crystal structure of chaperonin-60 from Paracoccus denitrificans, (P.cpn60) has been determined at 3.2 A resolution by the molecular, replacement method. Two heptameric rings of identical subunits of P.cpn60, in adjacent asymmetric units are stacked in a back-to-back manner and form, a cylinder, as found in GroEL, cpn60 from Escherichia coli. With respect, to the unliganded GroEL structure, each subunit of P.cpn60 tilts 2 degrees, outwards and the apical domain twists 4 degrees counter-clockwise in the, top view in a hinge-like manner, rendering the central hole 5 A wider., Despite the subunit tilts, both rings in P.cpn60 contact at two sites of, the equatorial domain in the same way as in GroEL. Interactions between, residues 434 and 434, and 463 and 463 observed in GroEL were not found in, P.cpn60, and the interaction between 452 and 461 was weaker in P.cpn60, than in GroEL. The unique hydrogen bond between 468 and 471 was observed, at the right site in P.cpn60, which could account for why the subunits, tilt outwards. The contact surface area was reduced at the left site, which is similar to the observed changes in the GroEL structures induced, by ATP binding. In general, inter-ring interactions in P.cpn60 were, weakened, which is consistent with findings that P.cpn60 is observed in, single-ring forms as well as in double-ring forms.
About this Structure
1IOK is a Single protein structure of sequence from Paracoccus denitrificans. Full crystallographic information is available from OCA.
Reference
Crystal structure of chaperonin-60 from Paracoccus denitrificans., Fukami TA, Yohda M, Taguchi H, Yoshida M, Miki K, J Mol Biol. 2001 Sep 21;312(3):501-9. PMID:11563912
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