1xck: Difference between revisions
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[[Image:1xck.gif|left|200px]] | [[Image:1xck.gif|left|200px]] | ||
'''Crystal structure of apo GroEL''' | {{Structure | ||
|PDB= 1xck |SIZE=350|CAPTION= <scene name='initialview01'>1xck</scene>, resolution 2.92Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene> and <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of apo GroEL''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1XCK is a [ | 1XCK is a [[Single protein]] structure of 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=1XCK OCA]. | ||
==Reference== | ==Reference== | ||
Crystal structure of wild-type chaperonin GroEL., Bartolucci C, Lamba D, Grazulis S, Manakova E, Heumann H, J Mol Biol. 2005 Dec 9;354(4):940-51. Epub 2005 Oct 21. PMID:[http:// | Crystal structure of wild-type chaperonin GroEL., Bartolucci C, Lamba D, Grazulis S, Manakova E, Heumann H, J Mol Biol. 2005 Dec 9;354(4):940-51. Epub 2005 Oct 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16288915 16288915] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: chaperonin]] | [[Category: chaperonin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:08:01 2008'' | ||
Revision as of 16:08, 20 March 2008
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| , resolution 2.92Å | |||||||
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| Ligands: | , , and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of apo GroEL
OverviewOverview
The 2.9A resolution crystal structure of apo wild-type GroEL was determined for the first time and represents the reference structure, facilitating the study of structural and functional differences observed in GroEL variants. Until now the crystal structure of the mutant Arg13Gly, Ala126Val GroEL was used for this purpose. We show that, due to the mutations as well as to the presence of a crystallographic symmetry, the ring-ring interface was inaccurately described. Analysis of the present structure allowed the definition of structural elements at this interface, essential for understanding the inter-ring allosteric signal transmission. We also show unambiguously that there is no ATP-induced 102 degrees rotation of the apical domain helix I around its helical axis, as previously assumed in the crystal structure of the (GroEL-KMgATP)(14) complex, and analyze the apical domain movements. These results enabled us to compare our structure with other GroEL crystal structures already published, allowing us to suggest a new route through which the allosteric signal for negative cooperativity propagates within the molecule. The proposed mechanism, supported by known mutagenesis data, underlines the importance of the switching of salt bridges.
About this StructureAbout this Structure
1XCK is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of wild-type chaperonin GroEL., Bartolucci C, Lamba D, Grazulis S, Manakova E, Heumann H, J Mol Biol. 2005 Dec 9;354(4):940-51. Epub 2005 Oct 21. PMID:16288915
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