1iok
From Proteopedia
(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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| - | [[Image:1iok.gif|left|200px]]<br /><applet load="1iok" size=" | + | [[Image:1iok.gif|left|200px]]<br /><applet load="1iok" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1iok, resolution 3.20Å" /> | caption="1iok, resolution 3.20Å" /> | ||
'''CRYSTAL STRUCTURE OF CHAPERONIN-60 FROM PARACOCCUS DENITRIFICANS'''<br /> | '''CRYSTAL STRUCTURE OF CHAPERONIN-60 FROM PARACOCCUS DENITRIFICANS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of chaperonin-60 from Paracoccus denitrificans | + | 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== | ==About this Structure== | ||
| - | 1IOK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http:// | + | 1IOK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Paracoccus_denitrificans Paracoccus denitrificans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IOK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Paracoccus denitrificans]] | [[Category: Paracoccus denitrificans]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Fukami, T | + | [[Category: Fukami, T A.]] |
[[Category: Miki, K.]] | [[Category: Miki, K.]] | ||
[[Category: Taguchi, H.]] | [[Category: Taguchi, H.]] | ||
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[[Category: chaperonin]] | [[Category: chaperonin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:56 2008'' |
Revision as of 11:14, 21 February 2008
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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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