1tg6: Difference between revisions

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[[Image:1tg6.gif|left|200px]]
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{{STRUCTURE_1tg6|  PDB=1tg6  |  SCENE=  }}  
{{STRUCTURE_1tg6|  PDB=1tg6  |  SCENE=  }}  


'''Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP'''
===Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP===




==Overview==
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We have determined a 2.1 A crystal structure for human mitochondrial ClpP (hClpP), the proteolytic component of the ATP-dependent ClpXP protease. HClpP has a structure similar to that of the bacterial enzyme, with the proteolytic active sites sequestered within an aqueous chamber formed by face-to-face assembly of the two heptameric rings. The hydrophobic N-terminal peptides of the subunits are bound within the narrow (12 A) axial channel, positioned to interact with unfolded substrates translocated there by the associated ClpX chaperone. Mutation or deletion of these residues causes a drastic decrease in ClpX-mediated protein and peptide degradation. Residues 8-16 form a mobile loop that extends above the ring surface and is also required for activity. The 28 amino acid C-terminal domain, a unique feature of mammalian ClpP proteins, lies on the periphery of the ring, with its proximal portion forming a loop that extends out from the ring surface. Residues at the start of the C-terminal domain impinge on subunit interfaces within the ring and affect heptamer assembly and stability. We propose that the N-terminal peptide of ClpP is a structural component of the substrate translocation channel and may play an important functional role as well.
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==About this Structure==
==About this Structure==
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[[Category: Mitochondrial clpp]]
[[Category: Mitochondrial clpp]]
[[Category: X-ray crystallography]]
[[Category: X-ray crystallography]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:54:53 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 12:35:53 2008''

Revision as of 09:35, 29 July 2008

File:1tg6.png

Template:STRUCTURE 1tg6

Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP

Template:ABSTRACT PUBMED 15522782

About this Structure

1TG6 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP., Kang SG, Maurizi MR, Thompson M, Mueser T, Ahvazi B, J Struct Biol. 2004 Dec;148(3):338-52. PMID:15522782

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