4p6y: Difference between revisions
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==Crystal structure of the M42 aminopeptidase TmPep1050 from Thermotoga maritima== | ==Crystal structure of the M42 aminopeptidase TmPep1050 from Thermotoga maritima== | ||
<StructureSection load='4p6y' size='340' side='right' caption='[[4p6y]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='4p6y' size='340' side='right'caption='[[4p6y]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4p6y]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P6Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P6Y FirstGlance]. <br> | <table><tr><td colspan='2'>[[4p6y]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4P6Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4P6Y FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3isx|3isx]], [[1xfo|1xfo]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3isx|3isx]], [[1xfo|1xfo]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_1050, THEMA_09110, Tmari_1054 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </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=4p6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p6y OCA], [http://pdbe.org/4p6y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p6y RCSB], [http://www.ebi.ac.uk/pdbsum/4p6y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p6y ProSAT]</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=4p6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p6y OCA], [http://pdbe.org/4p6y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4p6y RCSB], [http://www.ebi.ac.uk/pdbsum/4p6y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4p6y ProSAT]</span></td></tr> | ||
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</div> | </div> | ||
<div class="pdbe-citations 4p6y" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4p6y" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Cellulase]] | [[Category: Cellulase]] | ||
[[Category: Large Structures]] | |||
[[Category: Thema]] | |||
[[Category: Bauvois, C]] | [[Category: Bauvois, C]] | ||
[[Category: Demarez, M]] | [[Category: Demarez, M]] | ||
Revision as of 10:32, 17 April 2019
Crystal structure of the M42 aminopeptidase TmPep1050 from Thermotoga maritimaCrystal structure of the M42 aminopeptidase TmPep1050 from Thermotoga maritima
Structural highlights
Publication Abstract from PubMedSeveral aminopeptidases of the M42 family have been described as tetrahedral-shaped dodecameric (TET) aminopeptidases. A current hypothesis suggests that these enzymes are involved, along with the tricorn peptidase, in degrading peptides produced by the proteasome. Yet the M42 family remains ill defined, as some members have been annotated as cellulases because of their homology with CelM, formerly described as an endoglucanase of Clostridium thermocellum. Here we describe the catalytic functions and substrate profiles CelM and of TmPep1050, the latter having been annotated as an endoglucanase of Thermotoga maritima. Both enzymes were shown to catalyze hydrolysis of nonpolar aliphatic L-amino acid-pNA substrates, the L-leucine derivative appearing as the best substrate. No significant endoglucanase activity was measured, either for TmPep1050 or CelM. Addition of cobalt ions enhanced the activity of both enzymes significantly, while both the chelating agent EDTA and bestatin, a specific inhibitor of metalloaminopeptidases, proved inhibitory. Our results strongly suggest that one should avoid annotating members of the M42 aminopeptidase family as cellulases. In an updated assessment of the distribution of M42 aminopeptidases, we found TET aminopeptidases to be distributed widely amongst archaea and bacteria. We additionally observed that several phyla lack both TET and tricorn. This suggests that other complexes may act downstream from the proteasome. Functional characterization of two M42 aminopeptidases erroneously annotated as cellulases.,Dutoit R, Brandt N, Legrain C, Bauvois C PLoS One. 2012;7(11):e50639. doi: 10.1371/journal.pone.0050639. Epub 2012 Nov 30. PMID:23226342[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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