1mt3

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[[Image:1mt3.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of the Tricorn Interacting Factor Selenomethionine-F1==
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|PDB= 1mt3 |SIZE=350|CAPTION= <scene name='initialview01'>1mt3</scene>, resolution 2.0&Aring;
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<StructureSection load='1mt3' size='340' side='right'caption='[[1mt3]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>
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<table><tr><td colspan='2'>[[1mt3]] 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=1MT3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MT3 FirstGlance]. <br>
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|ACTIVITY= <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>
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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&#8491;</td></tr>
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|GENE= TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 Thermoplasma acidophilum])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1mt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mt3 OCA], [https://pdbe.org/1mt3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mt3 RCSB], [https://www.ebi.ac.uk/pdbsum/1mt3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mt3 ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1mtz|1MTZ]], [[1mu0|1MU0]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mt3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mt3 OCA], [http://www.ebi.ac.uk/pdbsum/1mt3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mt3 RCSB]</span>
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== Function ==
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}}
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[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.
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== Evolutionary Conservation ==
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'''Crystal Structure of the Tricorn Interacting Factor Selenomethionine-F1'''
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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/mt/1mt3_consurf.spt"</scriptWhenChecked>
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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.
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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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1MT3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MT3 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=1mt3 ConSurf].
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<div style="clear:both"></div>
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==Reference==
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__TOC__
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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:[http://www.ncbi.nlm.nih.gov/pubmed/12374735 12374735]
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</StructureSection>
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[[Category: Prolyl aminopeptidase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Thermoplasma acidophilum]]
[[Category: Thermoplasma acidophilum]]
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[[Category: Brandstetter, H.]]
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[[Category: Brandstetter H]]
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[[Category: Goettig, P.]]
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[[Category: Goettig P]]
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[[Category: Groll, M.]]
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[[Category: Groll M]]
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[[Category: Huber, R.]]
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[[Category: Huber R]]
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[[Category: Kim, J S.]]
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[[Category: Kim J-S]]
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[[Category: alpha-beta hydrolase]]
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[[Category: caged active site]]
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[[Category: cap domain]]
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[[Category: prolylpeptidase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:20:47 2008''
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Current revision

Crystal Structure of the Tricorn Interacting Factor Selenomethionine-F1

PDB ID 1mt3

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