1tg6
From Proteopedia
(New page: 200px<br /> <applet load="1tg6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tg6, resolution 2.10Å" /> '''Crystallography and...) |
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| - | [[Image:1tg6.gif|left|200px]]<br /> | + | [[Image:1tg6.gif|left|200px]]<br /><applet load="1tg6" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1tg6" size=" | + | |
caption="1tg6, resolution 2.10Å" /> | caption="1tg6, resolution 2.10Å" /> | ||
'''Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP'''<br /> | '''Crystallography and mutagenesis point to an essential role for the N-terminus of human mitochondrial ClpP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined a 2.1 A crystal structure for human mitochondrial ClpP | + | 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== | ==About this Structure== | ||
| - | 1TG6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with DIO, EDO, FME and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1TG6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=DIO:'>DIO</scene>, <scene name='pdbligand=EDO:'>EDO</scene>, <scene name='pdbligand=FME:'>FME</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TG6 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Ahvazi, B.]] | [[Category: Ahvazi, B.]] | ||
| - | [[Category: Kang, S | + | [[Category: Kang, S G.]] |
| - | [[Category: Maurizi, M | + | [[Category: Maurizi, M R.]] |
[[Category: Mueser, T.]] | [[Category: Mueser, T.]] | ||
[[Category: Thompson, M.]] | [[Category: Thompson, M.]] | ||
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[[Category: x-ray crystallography]] | [[Category: x-ray crystallography]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:13:11 2008'' |
Revision as of 13:13, 21 February 2008
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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 with , , and as ligands. Active as Endopeptidase Clp, with EC number 3.4.21.92 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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