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1hr6

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[[Image:1hr6.gif|left|200px]]
 
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{{Structure
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==Yeast Mitochondrial Processing Peptidase==
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|PDB= 1hr6 |SIZE=350|CAPTION= <scene name='initialview01'>1hr6</scene>, resolution 2.50&Aring;
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<StructureSection load='1hr6' size='340' side='right'caption='[[1hr6]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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<table><tr><td colspan='2'>[[1hr6]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HR6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HR6 FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Mitochondrial_processing_peptidase Mitochondrial processing peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.64 3.4.24.64] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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|DOMAIN=
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hr6 OCA], [https://pdbe.org/1hr6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hr6 RCSB], [https://www.ebi.ac.uk/pdbsum/1hr6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hr6 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1hr7|1HR7]], [[1hr8|1HR8]], [[1hr9|1HR9]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hr6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hr6 OCA], [http://www.ebi.ac.uk/pdbsum/1hr6 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hr6 RCSB]</span>
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== Function ==
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}}
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[https://www.uniprot.org/uniprot/MPPA_YEAST MPPA_YEAST] Cleaves presequences (transit peptides) from mitochondrial protein precursors. The cleavage sites typically contain an arginine at position -2 (in the N-terminal portion) from the scissible peptide bond in addition to other distal basic residues, and an aromatic residue at position +1.
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== Evolutionary Conservation ==
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'''YEAST MITOCHONDRIAL PROCESSING PEPTIDASE'''
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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==Overview==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hr/1hr6_consurf.spt"</scriptWhenChecked>
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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.
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==About this Structure==
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</jmolCheckbox>
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1HR6 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HR6 OCA].
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hr6 ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11470436 11470436]
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</StructureSection>
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[[Category: Mitochondrial processing peptidase]]
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[[Category: Large Structures]]
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[[Category: Protein complex]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Deisenhofer, J.]]
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[[Category: Deisenhofer J]]
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[[Category: Ito, A.]]
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[[Category: Ito A]]
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[[Category: Kitada, S.]]
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[[Category: Kitada S]]
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[[Category: Kojima, K.]]
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[[Category: Kojima K]]
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[[Category: Miyaura, H.]]
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[[Category: Miyaura H]]
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[[Category: Otwinowski, Z.]]
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[[Category: Otwinowski Z]]
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[[Category: Smith, B S.]]
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[[Category: Smith BS]]
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[[Category: Taylor, A B.]]
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[[Category: Taylor AB]]
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[[Category: hxxeh zinc-binding motif]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:09:20 2008''
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Current revision

Yeast Mitochondrial Processing Peptidase

PDB ID 1hr6

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