From Proteopedia
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| - | [[Image:1hr9.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1hr9| PDB=1hr9 | SCENE= }} | | {{STRUCTURE_1hr9| PDB=1hr9 | SCENE= }} |
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| - | '''Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Malate Dehydrogenase Signal Peptide'''
| + | ===Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Malate Dehydrogenase Signal Peptide=== |
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| - | ==Overview==
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| - | BACKGROUND: Mitochondrial processing peptidase (MPP) is a metalloendopeptidase that cleaves the N-terminal signal sequences of nuclear-encoded proteins targeted for transport from the cytosol to the mitochondria. Mitochondrial signal sequences vary in length and sequence, but each is cleaved at a single specific site by MPP. The cleavage sites typically contain an arginine at position -2 (in the N-terminal portion) from the scissile peptide bond in addition to other distal basic residues, and an aromatic residue at position +1. Mitochondrial import machinery recognizes amphiphilic helical conformations in signal sequences. However, it is unclear how MPP specifically recognizes diverse presequence substrates. RESULTS: The crystal structures of recombinant yeast MPP and a cleavage-deficient mutant of MPP complexed with synthetic signal peptides have been determined. MPP is a heterodimer; its alpha and beta subunits are homologous to the core II and core I proteins, respectively, of the ubiquinol-cytochrome c oxidoreductase complex. Crystal structures of two different synthetic substrate peptides cocrystallized with the mutant MPP each show the peptide bound in an extended conformation at the active site. Recognition sites for the arginine at position -2 and the +1 aromatic residue are observed. CONCLUSIONS: MPP bound two mitochondrial import presequence peptides in extended conformations in a large polar cavity. The presequence conformations differ from the amphiphilic helical conformation recognized by mitochondrial import components. Our findings suggest that the presequences adopt context-dependent conformations through mitochondrial import and processing, helical for recognition by mitochondrial import machinery and extended for cleavage by the main processing component.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_11470436}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11470436 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11470436}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hxxeh zinc-binding motif]] | | [[Category: Hxxeh zinc-binding motif]] |
| | [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 7 08:40:24 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:34:33 2008'' |
Revision as of 05:34, 1 July 2008
Template:STRUCTURE 1hr9
Yeast Mitochondrial Processing Peptidase beta-E73Q Mutant Complexed with Malate Dehydrogenase Signal Peptide
Template:ABSTRACT PUBMED 11470436
About this Structure
1HR9 is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structures of mitochondrial processing peptidase reveal the mode for specific cleavage of import signal sequences., Taylor AB, Smith BS, Kitada S, Kojima K, Miyaura H, Otwinowski Z, Ito A, Deisenhofer J, Structure. 2001 Jul 3;9(7):615-25. PMID:11470436
Page seeded by OCA on Tue Jul 1 08:34:33 2008
