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| - | [[Image:1yg6.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1yg6.png|left|200px]] |
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| | {{STRUCTURE_1yg6| PDB=1yg6 | SCENE= }} | | {{STRUCTURE_1yg6| PDB=1yg6 | SCENE= }} |
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| - | '''ClpP'''
| + | ===ClpP=== |
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| - | ==Overview==
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| - | ClpP is a self-compartmentalized proteolytic assembly comprised of two, stacked, heptameric rings that, when associated with its cognate hexameric ATPase (ClpA or ClpX), form the ClpAP and ClpXP ATP-dependent protease, respectively. The symmetry mismatch is an absolute feature of this large energy-dependent protease and also of the proteasome, which shares a similar barrel-shaped architecture, but how it is accommodated within the complex has yet to be understood, despite recent structural investigations, due in part to the conformational lability of the N-termini. We present the structures of Escherichia coli ClpP to 1.9A and an inactive variant that provide some clues for how this might be achieved. In the wild type protein, the highly conserved N-terminal 20 residues can be grouped into two major structural classes. In the first, a loop formed by residues 10-15 protrudes out of the central access channel extending approximately 12-15A from the surface of the oligomer resulting in the closing of the access channel observed in one ring. Similar loops are implied to be exclusively observed in human ClpP and a variant of ClpP from Streptococcus pneumoniae. In the other ring, a second class of loop is visible in the structure of wt ClpP from E. coli that forms closer to residue 16 and faces toward the interior of the molecule creating an open conformation of the access channel. In both classes, residues 18-20 provide a conserved interaction surface. In the inactive variant, a third class of N-terminal conformation is observed, which arises from a conformational change in the position of F17. We have performed a detailed functional analysis on each of the first 20 amino acid residues of ClpP. Residues that extend beyond the plane of the molecule (10-15) have a lesser effect on ATPase interaction than those lining the pore (1-7 and 16-20). Based upon our structure-function analysis, we present a model to explain the widely disparate effects of individual residues on ClpP-ATPase complex formation and also a possible functional reason for this mismatch.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16406682}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16406682 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16406682}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Heat shock protein f21 5]] | | [[Category: Heat shock protein f21 5]] |
| | [[Category: Protease ti]] | | [[Category: Protease ti]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:16:42 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:56:14 2008'' |
Revision as of 07:56, 29 July 2008
Template:STRUCTURE 1yg6
ClpP
Template:ABSTRACT PUBMED 16406682
About this Structure
1YG6 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
The asymmetry in the mature amino-terminus of ClpP facilitates a local symmetry match in ClpAP and ClpXP complexes., Bewley MC, Graziano V, Griffin K, Flanagan JM, J Struct Biol. 2006 Feb;153(2):113-28. Epub 2005 Dec 1. PMID:16406682
Page seeded by OCA on Tue Jul 29 10:56:14 2008
