We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1q3s

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1q3s.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1q3s.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1q3s| PDB=1q3s | SCENE= }}
{{STRUCTURE_1q3s| PDB=1q3s | SCENE= }}
-
'''Crystal structure of the chaperonin from Thermococcus strain KS-1 (FormIII crystal complexed with ADP)'''
+
===Crystal structure of the chaperonin from Thermococcus strain KS-1 (FormIII crystal complexed with ADP)===
-
==Overview==
+
<!--
-
The crystal structures of the group II chaperonins consisting of the alpha subunit with amino acid substitutions of G65C and/or I125T from the hyperthermophilic archaeum Thermococcus strain KS-1 were determined. These mutants have been shown to be active in ATP hydrolysis but inactive in protein folding. The structures were shown to be double-ring hexadecamers in an extremely closed form, which was consistent with the crystal structure of native alpha8beta8-chaperonin from Thermoplasma acidophilum. Comparisons of the present structures with the atomic structures of the GroEL14-GroES7-(ADP)7 complex revealed that the deficiency in protein-folding activity with the G65C amino acid substitution is caused by the steric hindrance of the local conformational change in an equatorial domain. We concluded that this mutant chaperonin with G65C substitution is deprived of the smooth conformational change in the refolding-reaction cycle. We obtained a new form of crystal with a distinct space group at a lower concentration of sulfate ion in the presence of nucleotide. The crystal structure obtained at the lower concentration of sulfate ion tilts outward, and has much looser inter-subunit contacts compared with those in the presence of a higher concentration of sulfate ion. Such subunit rotation has never been characterized in group II chaperonins. The crystal structure obtained at the lower concentration of sulfate ion tilts outward, and has much looser inter-subunit contacts compared with those in the presence of a higher concentration of sulfate ion.
+
The line below this paragraph, {{ABSTRACT_PUBMED_14729342}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 14729342 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_14729342}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Chaperonin]]
[[Category: Chaperonin]]
[[Category: Thermosome]]
[[Category: Thermosome]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 05:49:58 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:04:40 2008''

Revision as of 12:04, 28 July 2008

Image:1q3s.png

Template:STRUCTURE 1q3s

Crystal structure of the chaperonin from Thermococcus strain KS-1 (FormIII crystal complexed with ADP)

Template:ABSTRACT PUBMED 14729342

About this Structure

1Q3S is a Single protein structure of sequence from Thermococcus sp.. Full crystallographic information is available from OCA.

Reference

Crystal structures of the group II chaperonin from Thermococcus strain KS-1: steric hindrance by the substituted amino acid, and inter-subunit rearrangement between two crystal forms., Shomura Y, Yoshida T, Iizuka R, Maruyama T, Yohda M, Miki K, J Mol Biol. 2004 Jan 30;335(5):1265-78. PMID:14729342

Page seeded by OCA on Mon Jul 28 15:04:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1q3s"
Personal tools