3TRS
The crystal structure of aspergilloglutamic peptidase from Aspergillus niger
Summary for 3TRS
| Entry DOI | 10.2210/pdb3trs/pdb |
| Descriptor | Aspergillopepsin-2 light chain, Aspergillopepsin-2 heavy chain, DIMETHYL SULFOXIDE, ... (4 entities in total) |
| Functional Keywords | aspergilloglutamic peptidase, glutamic peptidase, beta sandwich structure, hydrolase |
| Biological source | Aspergillus niger More |
| Total number of polymer chains | 4 |
| Total formula weight | 44739.09 |
| Authors | Sasaki, H.,Kubota, K.,Lee, W.C.,Ohtsuka, J.,Kojima, M.,Takahashi, K.,Tanokura, M. (deposition date: 2011-09-10, release date: 2012-08-22, Last modification date: 2024-11-20) |
| Primary citation | Sasaki, H.,Kubota, K.,Lee, W.C.,Ohtsuka, J.,Kojima, M.,Iwata, S.,Nakagawa, A.,Takahashi, K.,Tanokura, M. The crystal structure of an intermediate dimer of aspergilloglutamic peptidase that mimics the enzyme-activation product complex produced upon autoproteolysis. J.Biochem., 152:45-52, 2012 Cited by PubMed Abstract: 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 Å. 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. PubMed: 22569035DOI: 10.1093/jb/mvs050 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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