1tg6
From Proteopedia
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|PDB= 1tg6 |SIZE=350|CAPTION= <scene name='initialview01'>1tg6</scene>, resolution 2.10Å | |PDB= 1tg6 |SIZE=350|CAPTION= <scene name='initialview01'>1tg6</scene>, resolution 2.10Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene> | + | |LIGAND= <scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=FME:N-FORMYLMETHIONINE'>FME</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Endopeptidase_Clp Endopeptidase Clp], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.92 3.4.21.92] </span> |
|GENE= CLPP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= CLPP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1tyf|1TYF]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tg6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tg6 OCA], [http://www.ebi.ac.uk/pdbsum/1tg6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tg6 RCSB]</span> | ||
}} | }} | ||
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[[Category: Mueser, T.]] | [[Category: Mueser, T.]] | ||
[[Category: Thompson, M.]] | [[Category: Thompson, M.]] | ||
| - | [[Category: DIO]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: FME]] | ||
| - | [[Category: GOL]] | ||
[[Category: atp-dependent protease]] | [[Category: atp-dependent protease]] | ||
[[Category: clp/hsp 100]] | [[Category: clp/hsp 100]] | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:55:37 2008'' |
Revision as of 20:55, 30 March 2008
| |||||||
| , resolution 2.10Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | CLPP (Homo sapiens) | ||||||
| Activity: | Endopeptidase Clp, with EC number 3.4.21.92 | ||||||
| Related: | 1TYF
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP
Overview
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.
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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