1ss8
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= GROL, GROEL, MOPA, B4143, C5227, Z5748, ECS5124, SF4297, S4564 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | |GENE= GROL, GROEL, MOPA, B4143, C5227, Z5748, ECS5124, SF4297, S4564 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1oel|1OEL]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ss8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ss8 OCA], [http://www.ebi.ac.uk/pdbsum/1ss8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ss8 RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: protein folding]] | [[Category: protein folding]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:46:15 2008'' |
Revision as of 20:46, 30 March 2008
| |||||||
| , resolution 2.700Å | |||||||
|---|---|---|---|---|---|---|---|
| Gene: | GROL, GROEL, MOPA, B4143, C5227, Z5748, ECS5124, SF4297, S4564 (Escherichia coli) | ||||||
| Related: | 1OEL
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GroEL
Overview
Large rigid-body domain movements are critical to GroEL-mediated protein folding, especially apical domain elevation and twist associated with the formation of a folding chamber upon binding ATP and co-chaperonin GroES. Here, we have modeled the anisotropic displacements of GroEL domains from various crystallized states, unliganded GroEL, ATPgammaS-bound, ADP-AlFx/GroES-bound, and ADP/GroES bound, using translation-libration-screw (TLS) analysis. Remarkably, the TLS results show that the inherent motions of unliganded GroEL, a polypeptide-accepting state, are biased along the transition pathway that leads to the folding-active state. In the ADP-AlFx/GroES-bound folding-active state the dynamic modes of the apical domains become reoriented and coupled to the motions of bound GroES. The ADP/GroES complex exhibits these same motions, but they are increased in magnitude, potentially reflecting the decreased stability of the complex after nucleotide hydrolysis. Our results have allowed the visualization of the anisotropic molecular motions that link the static conformations previously observed by X-ray crystallography. Application of the same analyses to other macromolecules where rigid body motions occur may give insight into the large scale dynamics critical for function and thus has the potential to extend our fundamental understanding of molecular machines.
About this Structure
1SS8 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Exploring the structural dynamics of the E.coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states., Chaudhry C, Horwich AL, Brunger AT, Adams PD, J Mol Biol. 2004 Sep 3;342(1):229-45. PMID:15313620
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