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| | <StructureSection load='5ne7' size='340' side='right'caption='[[5ne7]], [[Resolution|resolution]] 1.84Å' scene=''> | | <StructureSection load='5ne7' size='340' side='right'caption='[[5ne7]], [[Resolution|resolution]] 1.84Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ne7]] is a 2 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=5NE7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NE7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ne7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NE7 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</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]] 1.84Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TM_1050, Tmari_1054 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Leucyl_aminopeptidase Leucyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.1 3.4.11.1] </span></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=5ne7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ne7 OCA], [https://pdbe.org/5ne7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ne7 RCSB], [https://www.ebi.ac.uk/pdbsum/5ne7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ne7 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=5ne7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ne7 OCA], [http://pdbe.org/5ne7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ne7 RCSB], [http://www.ebi.ac.uk/pdbsum/5ne7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ne7 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9X0E0_THEMA Q9X0E0_THEMA] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Leucyl aminopeptidase]] | + | [[Category: Thermotoga maritima MSB8]] |
| - | [[Category: Thema]]
| + | [[Category: Dutoit R]] |
| - | [[Category: Dutoit, R]] | + | |
| - | [[Category: Aminopeptidase]]
| + | |
| - | [[Category: Lyase]]
| + | |
| - | [[Category: M42 family]]
| + | |
| - | [[Category: Metal ion binding]]
| + | |
| - | [[Category: Tetrahedral structure]]
| + | |
| Structural highlights
Function
Q9X0E0_THEMA
Publication Abstract from PubMed
The M42 aminopeptidases are dinuclear aminopeptidases displaying a peculiar tetrahedral-shaped structure with twelve subunits. Their quaternary structure results from the self-assembly of six dimers controlled by their divalent metal ion cofactors. The oligomeric state transition remains debated despite the structural characterization of several archaeal M42 aminopeptidases. The main bottleneck is the lack of dimer structures, hindering the understanding of structural changes occurring during the oligomerization process. We present the first dimer structure of an M42 aminopeptidase, TmPep1050 of Thermotoga maritima, along with the dodecamer structure. The comparison of both structures allows to describe how the metal ion cofactors modulate the active site fold and, subsequently, affect the interaction interface between dimers. A mutational study shows that the M1 site strictly controls dodecamer formation. The dodecamer structure of TmPep1050 also reveals that a part of the dimerization domain delimits the catalytic pocket and could participate in substrate binding.
How metal cofactors drive dimer-dodecamer transition of the M42 aminopeptidase TmPep1050 of Thermotoga maritima.,Dutoit R, Van Gompel T, Brandt N, Van Elder D, Van Dyck J, Sobott F, Droogmans L J Biol Chem. 2019 Oct 14. pii: RA119.009281. doi: 10.1074/jbc.RA119.009281. PMID:31611236[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Dutoit R, Van Gompel T, Brandt N, Van Elder D, Van Dyck J, Sobott F, Droogmans L. How metal cofactors drive dimer-dodecamer transition of the M42 aminopeptidase TmPep1050 of Thermotoga maritima. J Biol Chem. 2019 Oct 14. pii: RA119.009281. doi: 10.1074/jbc.RA119.009281. PMID:31611236 doi:http://dx.doi.org/10.1074/jbc.RA119.009281
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