4aas

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[[Image:4aas.jpg|left|200px]]
 
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{{STRUCTURE_4aas| PDB=4aas | SCENE= }}
{{STRUCTURE_4aas| PDB=4aas | SCENE= }}
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===ATP-triggered molecular mechanics of the chaperonin GroEL===
===ATP-triggered molecular mechanics of the chaperonin GroEL===
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{{ABSTRACT_PUBMED_22445172}}
{{ABSTRACT_PUBMED_22445172}}
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==Function==
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[[http://www.uniprot.org/uniprot/CH60_ECOLI CH60_ECOLI]] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600] Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600]
==About this Structure==
==About this Structure==
[[4aas]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AAS OCA].
[[4aas]] is a 14 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AAS OCA].
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==See Also==
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*[[Chaperonin|Chaperonin]]
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==Reference==
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<ref group="xtra">PMID:022445172</ref><references group="xtra"/><references/>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Clare, D K.]]
[[Category: Clare, D K.]]

Revision as of 06:40, 29 September 2013

Template:STRUCTURE 4aas

Contents

ATP-triggered molecular mechanics of the chaperonin GroEL

Template:ABSTRACT PUBMED 22445172

Function

[CH60_ECOLI] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.[HAMAP-Rule:MF_00600] Essential for the growth of the bacteria and the assembly of several bacteriophages. Also plays a role in coupling between replication of the F plasmid and cell division of the cell.[HAMAP-Rule:MF_00600]

About this Structure

4aas is a 14 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA.

See Also

Reference

  • Clare DK, Vasishtan D, Stagg S, Quispe J, Farr GW, Topf M, Horwich AL, Saibil HR. ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin. Cell. 2012 Mar 30;149(1):113-23. Epub 2012 Mar 22. PMID:22445172 doi:10.1016/j.cell.2012.02.047

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