Summary for 2R33
| Entry DOI | 10.2210/pdb2r33/pdb |
| Related | 2OT6 |
| Descriptor | Bowman-Birk type seed trypsin and chymotrypsin inhibitor (2 entities in total) |
| Functional Keywords | bowman-birk protease inhibitor, vigna unguiculata, plant-pis, protein-protein interactions, serine protease inhibitor, plant protein |
| Biological source | Vigna unguiculata (cowpea) |
| Total number of polymer chains | 2 |
| Total formula weight | 16006.12 |
| Authors | Rao, K.N.,Suresh, C.G. (deposition date: 2007-08-28, release date: 2007-11-27, Last modification date: 2024-11-06) |
| Primary citation | Rao, K.N.,Suresh, C.G. Bowman-Birk protease inhibitor from the seeds of Vigna unguiculata forms a highly stable dimeric structure. Biochim.Biophys.Acta, 1774:1264-1273, 2007 Cited by PubMed Abstract: Different protease inhibitors including Bowman-Birk type (BBI) have been reported from the seeds of Vigna unguiculata. Protease isoinhibitors of double-headed Bowman-Birk type from the seeds of Vigna unguiculata have been purified and characterized. The BBI from Vigna unguiculata (Vu-BBI) has been found to undergo self-association to form very stable dimers and more complex oligomers, by size-exclusion chromatography and SDS-PAGE in the presence of urea. Many BBIs have been reported to undergo self-association to form homodimers or more complex oligomers in solution. Only one dimeric crystal structure of a BBI (pea-BBI) is reported to date. We report the three-dimensional structure of a Vu-BBI determined at 2.5 A resolution. Although, the inhibitor has a monomer fold similar to that found in other known structures of Bowman-Birk protease inhibitors, its quaternary structure is different from that commonly observed in this family. The structural elements responsible for the stability of monomer molecule and dimeric association are discussed. The Vu-BBI may use dimeric or higher quaternary association to maintain the physiological state and to execute its biological function. PubMed: 17869196DOI: 10.1016/j.bbapap.2007.07.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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