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| | ==Crystal Structure of the Tricorn Interacting Factor F1 Complex with PCK== | | ==Crystal Structure of the Tricorn Interacting Factor F1 Complex with PCK== |
| - | <StructureSection load='1mu0' size='340' side='right' caption='[[1mu0]], [[Resolution|resolution]] 2.40Å' scene=''> | + | <StructureSection load='1mu0' size='340' side='right'caption='[[1mu0]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1mu0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MU0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MU0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1mu0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MU0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PHK:(2R,3S)-3-AMINO-1-CHLORO-4-PHENYL-BUTAN-2-OL'>PHK</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mt3|1mt3]], [[1mtz|1mtz]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PHK:(2R,3S)-3-AMINO-1-CHLORO-4-PHENYL-BUTAN-2-OL'>PHK</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mu0 OCA], [https://pdbe.org/1mu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mu0 RCSB], [https://www.ebi.ac.uk/pdbsum/1mu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mu0 ProSAT]</span></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr>
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| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mu0 OCA], [http://pdbe.org/1mu0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mu0 RCSB], [http://www.ebi.ac.uk/pdbsum/1mu0 PDBsum]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PIP_THEAC PIP_THEAC]] Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome) yielding free amino acids. | + | [https://www.uniprot.org/uniprot/PIP_THEAC PIP_THEAC] Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome) yielding free amino acids. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| | Check<jmol> | | Check<jmol> |
| | <jmolCheckbox> | | <jmolCheckbox> |
| - | <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mu/1mu0_consurf.spt"</scriptWhenChecked> | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mu/1mu0_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Prolyl aminopeptidase]] | + | [[Category: Large Structures]] |
| - | [[Category: Brandstetter, H]] | + | [[Category: Thermoplasma acidophilum]] |
| - | [[Category: Goettig, P]] | + | [[Category: Brandstetter H]] |
| - | [[Category: Groll, M]] | + | [[Category: Goettig P]] |
| - | [[Category: Huber, R]] | + | [[Category: Groll M]] |
| - | [[Category: Kim, J S]] | + | [[Category: Huber R]] |
| - | [[Category: Alpha-beta hydrolase]]
| + | [[Category: Kim J-S]] |
| - | [[Category: Caged active site]]
| + | |
| - | [[Category: Cap domain]]
| + | |
| - | [[Category: Hydrolase]]
| + | |
| - | [[Category: Prolyl peptidase]]
| + | |
| Structural highlights
Function
PIP_THEAC Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome) yielding free amino acids.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
F1 is a 33.5 kDa serine peptidase of the alpha/beta-hydrolase family from the archaeon Thermoplasma acidophilum. Subsequent to proteasomal protein degradation, tricorn generates small peptides, which are cleaved by F1 to yield single amino acids. We have solved the crystal structure of F1 with multiwavelength anomalous dispersion (MAD) phasing at 1.8 A resolution. In addition to the conserved catalytic domain, the structure reveals a chiefly alpha-helical domain capping the catalytic triad. Thus, the active site is accessible only through a narrow opening from the protein surface. Two structures with molecules bound to the active serine, including the inhibitor phenylalanyl chloromethylketone, elucidate the N-terminal recognition of substrates and the catalytic activation switch mechanism of F1. The cap domain mainly confers the specificity for hydrophobic side chains by a novel cavity system, which, analogously to the tricorn protease, guides substrates to the buried active site and products away from it. Finally, the structure of F1 suggests a possible functional complex with tricorn that allows efficient processive degradation to free amino acids for cellular recycling.
Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism.,Goettig P, Groll M, Kim JS, Huber R, Brandstetter H EMBO J. 2002 Oct 15;21(20):5343-52. PMID:12374735[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goettig P, Groll M, Kim JS, Huber R, Brandstetter H. Structures of the tricorn-interacting aminopeptidase F1 with different ligands explain its catalytic mechanism. EMBO J. 2002 Oct 15;21(20):5343-52. PMID:12374735
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