3trs
From Proteopedia
(Difference between revisions)
| (5 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | The | + | ==The crystal structure of aspergilloglutamic peptidase from Aspergillus niger== |
| + | <StructureSection load='3trs' size='340' side='right'caption='[[3trs]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3trs]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_niger_var._macrosporus Aspergillus niger var. macrosporus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TRS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TRS FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></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=3trs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3trs OCA], [https://pdbe.org/3trs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3trs RCSB], [https://www.ebi.ac.uk/pdbsum/3trs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3trs ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PRTA_ASPNG PRTA_ASPNG] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Aspergilloglutamic peptidase from Aspergillus niger var. macrosporus (AGP) is one of the so-called pepstatin-insensitive acid endopeptidases, which are distinct from the well-studied aspartic peptidases. Among the known homologues of the glutamic peptidases, AGP is a unique two-chain enzyme with a light chain and a heavy chain bound non-covalently with each other, and thus is an interesting target for protein structure-function relationship studies. In this article, we report the crystal structure of a dimeric form of the enzyme at a resolution of 1.6 A. This form has a unique structure in which the C-terminal region of the light chain of one of the molecules binds to the active site cleft of the other molecule like a part of a substrate. This form mimics the enzyme-activation product complex produced upon autoproteolysis, and provides a structural clue that could help to clarify the activation mechanism. This type of dimeric structure of a peptidase is here reported for the first time. | ||
| - | + | The crystal structure of an intermediate dimer of aspergilloglutamic peptidase that mimics the enzyme-activation product complex produced upon autoproteolysis.,Sasaki H, Kubota K, Lee WC, Ohtsuka J, Kojima M, Iwata S, Nakagawa A, Takahashi K, Tanokura M J Biochem. 2012 Jul;152(1):45-52. Epub 2012 May 7. PMID:22569035<ref>PMID:22569035</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3trs" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Aspergillus niger var. macrosporus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kojima M]] | ||
| + | [[Category: Kubota K]] | ||
| + | [[Category: Lee WC]] | ||
| + | [[Category: Ohtsuka J]] | ||
| + | [[Category: Sasaki H]] | ||
| + | [[Category: Takahashi K]] | ||
| + | [[Category: Tanokura M]] | ||
Current revision
The crystal structure of aspergilloglutamic peptidase from Aspergillus niger
| |||||||||||
