2fge

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[[Image:2fge.gif|left|200px]]
[[Image:2fge.gif|left|200px]]
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{{Structure
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|PDB= 2fge |SIZE=350|CAPTION= <scene name='initialview01'>2fge</scene>, resolution 2.100&Aring;
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The line below this paragraph, containing "STRUCTURE_2fge", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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{{STRUCTURE_2fge| PDB=2fge | SCENE= }}
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|RELATEDENTRY=[[1q2l|1Q2L]], [[1hr6|1HR6]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fge FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fge OCA], [http://www.ebi.ac.uk/pdbsum/2fge PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fge RCSB]</span>
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'''Crystal structure of presequence protease PreP from Arabidopsis thaliana'''
'''Crystal structure of presequence protease PreP from Arabidopsis thaliana'''
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[[Category: Eneqvist, T.]]
[[Category: Eneqvist, T.]]
[[Category: Johnson, K A.]]
[[Category: Johnson, K A.]]
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[[Category: peptidasome]]
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[[Category: Peptidasome]]
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[[Category: protease-peptide complex]]
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[[Category: Protease-peptide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:51:43 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:02:22 2008''
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Revision as of 00:51, 4 May 2008

Template:STRUCTURE 2fge

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. 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 Page seeded by OCA on Sun May 4 03:51:43 2008

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