1we3: Difference between revisions

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~~'''~~Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus~~'''~~

===Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus===

~~==Overview==~~

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The ~~chaperonins GroEL and GroES are essential mediators of protein folding. GroEL binds nonnative protein~~, ~~ATP~~, ~~and GroES, generating a ternary complex in which protein folding occurs within~~ the ~~cavity capped by GroES~~ (~~cis-cavity). We determined the crystal structure of the native GroEL-GroES-ADP homolog from Thermus thermophilus, with substrate proteins in the cis-cavity,~~ at 2.~~8 A resolution~~. ~~Twenty-four in vivo substrate proteins within the cis-cavity were identified from the crystals. The structure around the cis-cavity, which encapsulates substrate proteins~~, ~~shows significant differences from that observed for~~ the ~~substrate-free Escherichia coli GroEL-GroES complex~~. ~~The apical domain around the cis~~-~~cavity of the Thermus GroEL~~-GroES complex exhibits a large deviation from the 7-fold symmetry. As a result, the GroEL-GroES interface differs considerably from the previously reported E. coli GroEL-GroES complex, including a previously unknown contact between GroEL and GroES.

The line below this paragraph, {{ABSTRACT_PUBMED_15296740}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 15296740 is the PubMed ID number.

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==About this Structure==

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[[Category: Hsp10]]

[[Category: Hsp60]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 13~~:31:34 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:09:23 2008''

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-[[Image:1we3.jpg|left|200px]]
+{{Seed}}
+[[Image:1we3.png|left|200px]]
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 {{STRUCTURE_1we3|  PDB=1we3  |  SCENE=  }}
-'''Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus'''
+===Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus===
-==Overview==
+<!--
-The chaperonins GroEL and GroES are essential mediators of protein folding. GroEL binds nonnative protein, ATP, and GroES, generating a ternary complex in which protein folding occurs within the cavity capped by GroES (cis-cavity). We determined the crystal structure of the native GroEL-GroES-ADP homolog from Thermus thermophilus, with substrate proteins in the cis-cavity, at 2.8 A resolution. Twenty-four in vivo substrate proteins within the cis-cavity were identified from the crystals. The structure around the cis-cavity, which encapsulates substrate proteins, shows significant differences from that observed for the substrate-free Escherichia coli GroEL-GroES complex. The apical domain around the cis-cavity of the Thermus GroEL-GroES complex exhibits a large deviation from the 7-fold symmetry. As a result, the GroEL-GroES interface differs considerably from the previously reported E. coli GroEL-GroES complex, including a previously unknown contact between GroEL and GroES.
+The line below this paragraph, {{ABSTRACT_PUBMED_15296740}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15296740 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15296740}}
 ==About this Structure==
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 [[Category: Hsp10]]
 [[Category: Hsp60]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 13:31:34 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:09:23 2008''