1kp8

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(New page: 200px<br /><applet load="1kp8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kp8, resolution 2.00&Aring;" /> '''Structural Basis for...)
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'''Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution'''<br />
'''Structural Basis for GroEL-assisted Protein Folding from the Crystal Structure of (GroEL-KMgATP)14 at 2.0 A Resolution'''<br />
==Overview==
==Overview==
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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.
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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 Structure==
==About this Structure==
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1KP8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with K, SO4, MG and ATP as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds the now removed PDB entry 1DER. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KP8 OCA].
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1KP8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ATP:'>ATP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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].
==Reference==
==Reference==
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[[Category: groel]]
[[Category: groel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:33:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:36:28 2008''

Revision as of 11:36, 21 February 2008

Image:1kp8.gif

1kp8, resolution 2.00Å

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

Overview

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 Structure

1KP8 is a Single protein structure of sequence from Escherichia coli with , , and as ligands. This structure supersedes the now removed PDB entry 1DER. Full crystallographic information is available from OCA.

Reference

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

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