1xrm

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[[Image:1xrm.gif|left|200px]]
 
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{{Structure
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==Crystal structure of active site F1-mutant E213Q soaked with peptide Ala-Phe==
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|PDB= 1xrm |SIZE=350|CAPTION= <scene name='initialview01'>1xrm</scene>, resolution 2.70&Aring;
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<StructureSection load='1xrm' size='340' side='right'caption='[[1xrm]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</scene>
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<table><tr><td colspan='2'>[[1xrm]] 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=1XRM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XRM 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]] 2.7&#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=ALA:ALANINE'>ALA</scene>, <scene name='pdbligand=PHE:PHENYLALANINE'>PHE</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=1xrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrm OCA], [https://pdbe.org/1xrm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xrm RCSB], [https://www.ebi.ac.uk/pdbsum/1xrm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xrm ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1mtz|1MTZ]], [[1mu0|1MU0]], [[1mt3|1MT3]], [[1xqv|1XQV]], [[1xqw|1XQW]], [[1xqx|1XQX]], [[1xqy|1XQY]], [[1xrl|1XRL]], [[1xrn|1XRN]], [[1xro|1XRO]], [[1xrp|1XRP]], [[1xrq|1XRQ]], [[1xrr|1XRR]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xrm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrm OCA], [http://www.ebi.ac.uk/pdbsum/1xrm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1xrm 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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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/xr/1xrm_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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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=1xrm ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The tricorn-interacting factor F1 of the archaeon Thermoplasma acidophilum cleaves small hydrophobic peptide products of the proteasome and tricorn protease. F1 mutants of the active site residues that are involved in substrate recognition and catalysis displayed distinct activity patterns toward fluorogenic test substrates. Crystal structures of the mutant proteins complexed with peptides Phe-Leu, Pro-Pro, or Pro-Leu-Gly-Gly showed interaction of glutamates 213 and 245 with the N termini of the peptides and defined the S1 and S1' sites and the role of the catalytic residues. Evidence was found for processive peptide cleavage in the N-to-C direction, whereby the P1' product is translocated into the S1 site. A functional interaction of F1 with the tricorn protease was observed with the inactive F1 mutant G37A. Moreover, small angle x-ray scattering measurements for tricorn and inhibited F1 have been interpreted as formation of transient and substrate-induced complexes.
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'''Crystal structure of active site F1-mutant E213Q soaked with peptide Ala-Phe'''
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X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum.,Goettig P, Brandstetter H, Groll M, Gohring W, Konarev PV, Svergun DI, Huber R, Kim JS J Biol Chem. 2005 Sep 30;280(39):33387-96. Epub 2005 Jul 1. PMID:15994304<ref>PMID:15994304</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1xrm" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The tricorn-interacting factor F1 of the archaeon Thermoplasma acidophilum cleaves small hydrophobic peptide products of the proteasome and tricorn protease. F1 mutants of the active site residues that are involved in substrate recognition and catalysis displayed distinct activity patterns toward fluorogenic test substrates. Crystal structures of the mutant proteins complexed with peptides Phe-Leu, Pro-Pro, or Pro-Leu-Gly-Gly showed interaction of glutamates 213 and 245 with the N termini of the peptides and defined the S1 and S1' sites and the role of the catalytic residues. Evidence was found for processive peptide cleavage in the N-to-C direction, whereby the P1' product is translocated into the S1 site. A functional interaction of F1 with the tricorn protease was observed with the inactive F1 mutant G37A. Moreover, small angle x-ray scattering measurements for tricorn and inhibited F1 have been interpreted as formation of transient and substrate-induced complexes.
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*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1XRM 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=1XRM OCA].
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__TOC__
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</StructureSection>
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==Reference==
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[[Category: Large Structures]]
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X-ray snapshots of peptide processing in mutants of tricorn-interacting factor F1 from Thermoplasma acidophilum., Goettig P, Brandstetter H, Groll M, Gohring W, Konarev PV, Svergun DI, Huber R, Kim JS, J Biol Chem. 2005 Sep 30;280(39):33387-96. Epub 2005 Jul 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15994304 15994304]
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[[Category: Prolyl aminopeptidase]]
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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: Goehring, W.]]
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[[Category: Goehring W]]
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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: Konarev, P V.]]
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[[Category: Konarev PV]]
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[[Category: Svergun, D I.]]
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[[Category: Svergun DI]]
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[[Category: alpha-beta hydrolase]]
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[[Category: caged active site]]
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[[Category: hydrogen bonded network]]
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[[Category: peptide cleavage]]
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[[Category: substrate recognition]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:53:44 2008''
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Current revision

Crystal structure of active site F1-mutant E213Q soaked with peptide Ala-Phe

PDB ID 1xrm

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