1kp8: Difference between revisions

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[[Image:1kp8.gif|left|200px]]
[[Image:1kp8.gif|left|200px]]


{{Structure
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|RELATEDENTRY=[[1kpo|1KPO]], [[1j4z|1J4Z]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kp8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kp8 OCA], [http://www.ebi.ac.uk/pdbsum/1kp8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1kp8 RCSB]</span>
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'''Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution'''
'''Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution'''
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==About this Structure==
==About this Structure==
1KP8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry 1DER. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KP8 OCA].  
1KP8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1der 1der]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KP8 OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Wang, J.]]
[[Category: Wang, J.]]
[[Category: assisted protein folding]]
[[Category: Assisted protein folding]]
[[Category: chaperonin]]
[[Category: Chaperonin]]
[[Category: groel]]
[[Category: Groel]]
 
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Revision as of 23:00, 2 May 2008

File:1kp8.gif

Template:STRUCTURE 1kp8

Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution


OverviewOverview

Nucleotide regulates the affinity of the bacterial chaperonin GroEL for protein substrates. GroEL binds protein substrates with high affinity in the absence of ATP and with low affinity in its presence. We report the crystal structure of (GroEL-KMgATP)(14) refined to 2.0 A resolution in which the ATP triphosphate moiety is directly coordinated by both K(+) and Mg(2+). Upon the binding of KMgATP, we observe previously unnoticed domain rotations and a 102 degrees rotation of the apical domain surface helix I. Two major consequences are a large lateral displacement of, and a dramatic reduction of hydrophobicity in, the apical domain surface. These results provide a basis for the nucleotide-dependent regulation of protein substrate binding and suggest a mechanism for GroEL-assisted protein folding by forced unfolding.

About this StructureAbout this Structure

1KP8 is a Single protein structure of sequence from Escherichia coli. This structure supersedes the now removed PDB entry 1der. Full crystallographic information is available from OCA.

ReferenceReference

Structural basis for GroEL-assisted protein folding from the crystal structure of (GroEL-KMgATP)14 at 2.0A resolution., Wang J, Boisvert DC, J Mol Biol. 2003 Apr 4;327(4):843-55. PMID:12654267 Page seeded by OCA on Fri May 2 23:00:18 2008

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