5Z6D
Crystal structure of Abundant Perithecial Protein (APP) from Neurospora crassa
Summary for 5Z6D
| Entry DOI | 10.2210/pdb5z6d/pdb |
| Descriptor | DUF1881 domain-containing protein (2 entities in total) |
| Functional Keywords | betagamma-crystallin domain, ig-like domain, abundant perithecial protein, metal binding protein |
| Biological source | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
| Total number of polymer chains | 2 |
| Total formula weight | 47754.50 |
| Authors | Srivastava, S.S.,Sankaranarayanan, R. (deposition date: 2018-01-22, release date: 2019-01-23, Last modification date: 2024-03-27) |
| Primary citation | Swaroop Srivastava, S.,Raman, R.,Kiran, U.,Garg, R.,Chadalawada, S.,Pawar, A.D.,Sankaranarayanan, R.,Sharma, Y. Interface interactions between beta gamma-crystallin domain and Ig-like domain render Ca2+-binding site inoperative in abundant perithecial protein of Neurospora crassa. Mol.Microbiol., 110:955-972, 2018 Cited by PubMed Abstract: We describe a set of proteins in which a βγ-crystallin domain pairs with an Ig-like domain, and which are confined to microbes, like bacteria, slime molds and fungi. DdCAD-1 (Ca -dependent cell adhesion molecule-1) and abundant perithecial protein (APP) represent this class of molecules. Using the crystal structure of APP-NTD (N-terminal domain of APP), we describe its mode of Ca binding and provide a generalized theme for correct identification of the Ca -binding site within this class of molecules. As a common feature, one of the two Ca -binding sites is non-functional in the βγ-crystallin domains of these proteins. While APP-NTD binds Ca with a micromolar affinity which is comparable to DdCAD-1, APP surprisingly does not bind Ca . Crystal structures of APP and Ca -bound APP-NTD reveal that the interface interactions in APP render its Ca -binding site inoperative. Thus, heterodomain association provides a novel mode of Ca -binding regulation in APP. Breaking the interface interactions (mutating Asp30Ala, Leu132Ala and Ile135Ala) or separation from the Ig-like domain removes the constraints upon the required conformational transition and enables the βγ-crystallin domain to bind Ca . In mechanistic detail, our work demonstrates an interdomain interface adapted to distinct functional niches in APP and its homolog DdCAD-1. PubMed: 30216631DOI: 10.1111/mmi.14130 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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