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1xro
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1xro]] is a 1 chain structure with 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=1XRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XRO FirstGlance]. <br> | <table><tr><td colspan='2'>[[1xro]] is a 1 chain structure with 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=1XRO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1XRO FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mtz|1mtz]], [[1mu0|1mu0]], [[1mt3|1mt3]], [[1xqv|1xqv]], [[1xqw|1xqw]], [[1xqx|1xqx]], [[1xqy|1xqy]], [[1xrl|1xrl]], [[1xrm|1xrm]], [[1xrn|1xrn]], [[1xrp|1xrp]], [[1xrq|1xrq]], [[1xrr|1xrr]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mtz|1mtz]], [[1mu0|1mu0]], [[1mt3|1mt3]], [[1xqv|1xqv]], [[1xqw|1xqw]], [[1xqx|1xqx]], [[1xqy|1xqy]], [[1xrl|1xrl]], [[1xrm|1xrm]], [[1xrn|1xrn]], [[1xrp|1xrp]], [[1xrq|1xrq]], [[1xrr|1xrr]]</td></tr> |
| - | <tr><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 acidophilum])</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 acidophilum])</td></tr> |
| - | <tr><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> | + | <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> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1xro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xro OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xro RCSB], [http://www.ebi.ac.uk/pdbsum/1xro PDBsum]</span></td></tr> | + | <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=1xro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xro OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1xro RCSB], [http://www.ebi.ac.uk/pdbsum/1xro PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == 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. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Prolyl aminopeptidase]] | [[Category: Prolyl aminopeptidase]] | ||
[[Category: Thermoplasma acidophilum]] | [[Category: Thermoplasma acidophilum]] | ||
| - | [[Category: Brandstetter, H | + | [[Category: Brandstetter, H]] |
| - | [[Category: Goehring, W | + | [[Category: Goehring, W]] |
| - | [[Category: Goettig, P | + | [[Category: Goettig, P]] |
| - | [[Category: Groll, M | + | [[Category: Groll, M]] |
| - | [[Category: Huber, R | + | [[Category: Huber, R]] |
| - | [[Category: Kim, J S | + | [[Category: Kim, J S]] |
| - | [[Category: Konarev, P V | + | [[Category: Konarev, P V]] |
| - | [[Category: Svergun, D I | + | [[Category: Svergun, D I]] |
[[Category: Alpha-beta hydrolase]] | [[Category: Alpha-beta hydrolase]] | ||
[[Category: Caged active site]] | [[Category: Caged active site]] | ||
Revision as of 18:10, 25 December 2014
Crystal structure of active site F1-mutant E213Q soaked with peptide Phe-Leu
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