2fge
From Proteopedia
(New page: 200px<br /><applet load="2fge" size="450" color="white" frame="true" align="right" spinBox="true" caption="2fge, resolution 2.100Å" /> '''Crystal structure o...) |
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| - | [[Image:2fge.gif|left|200px]]<br /><applet load="2fge" size=" | + | [[Image:2fge.gif|left|200px]]<br /><applet load="2fge" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2fge, resolution 2.100Å" /> | caption="2fge, resolution 2.100Å" /> | ||
'''Crystal structure of presequence protease PreP from Arabidopsis thaliana'''<br /> | '''Crystal structure of presequence protease PreP from Arabidopsis thaliana'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Presequence protease PreP is a novel protease that degrades targeting | + | Presequence protease PreP is a novel protease that degrades targeting peptides as well as other unstructured peptides in both mitochondria and chloroplasts. The first structure of PreP from Arabidopsis thaliana refined at 2.1 Angstroms resolution shows how the 995-residue polypeptide forms a unique proteolytic chamber of more than 10,000 Angstroms(3) in which the active site resides. Although there is no visible opening to the chamber, a peptide is bound to the active site. The closed conformation places previously unidentified residues from the C-terminal domain at the active site, separated by almost 800 residues in sequence to active site residues located in the N-terminal domain. Based on the structure, a novel mechanism for proteolysis is proposed involving hinge-bending motions that cause the protease to open and close in response to substrate binding. In support of this model, cysteine double mutants designed to keep the chamber covalently locked show no activity under oxidizing conditions. The manner in which substrates are processed inside the chamber is reminiscent of the proteasome; therefore, we refer to this protein as a peptidasome. |
==About this Structure== | ==About this Structure== | ||
| - | 2FGE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with ZN, CL and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2FGE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FGE OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Eneqvist, T.]] | [[Category: Eneqvist, T.]] | ||
| - | [[Category: Johnson, K | + | [[Category: Johnson, K A.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: MG]] | [[Category: MG]] | ||
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[[Category: peptidasome; protease-peptide complex]] | [[Category: peptidasome; protease-peptide complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:21:05 2008'' |
Revision as of 15:21, 21 February 2008
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Crystal structure of presequence protease PreP from Arabidopsis thaliana
Overview
Presequence protease PreP is a novel protease that degrades targeting peptides as well as other unstructured peptides in both mitochondria and chloroplasts. The first structure of PreP from Arabidopsis thaliana refined at 2.1 Angstroms resolution shows how the 995-residue polypeptide forms a unique proteolytic chamber of more than 10,000 Angstroms(3) in which the active site resides. Although there is no visible opening to the chamber, a peptide is bound to the active site. The closed conformation places previously unidentified residues from the C-terminal domain at the active site, separated by almost 800 residues in sequence to active site residues located in the N-terminal domain. Based on the structure, a novel mechanism for proteolysis is proposed involving hinge-bending motions that cause the protease to open and close in response to substrate binding. In support of this model, cysteine double mutants designed to keep the chamber covalently locked show no activity under oxidizing conditions. The manner in which substrates are processed inside the chamber is reminiscent of the proteasome; therefore, we refer to this protein as a peptidasome.
About this Structure
2FGE is a Single protein structure of sequence from Arabidopsis thaliana with , and as ligands. Full crystallographic information is available from OCA.
Reference
The closed structure of presequence protease PreP forms a unique 10,000 Angstroms3 chamber for proteolysis., Johnson KA, Bhushan S, Stahl A, Hallberg BM, Frohn A, Glaser E, Eneqvist T, EMBO J. 2006 May 3;25(9):1977-86. Epub 2006 Apr 6. PMID:16601675
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