1K9B
Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation
Summary for 1K9B
| Entry DOI | 10.2210/pdb1k9b/pdb |
| Related | 1BBI 1C2A 1D6R 1PBI 1PI2 |
| Descriptor | BOWMAN-BIRK TYPE PROTEINASE INHIBITOR (2 entities in total) |
| Functional Keywords | tripple-stranded beta hairpin, double-headed, hydrolase inhibitor |
| Biological source | Glycine max (soybean) |
| Total number of polymer chains | 1 |
| Total formula weight | 6431.54 |
| Authors | Voss, R.H.,Ermler, U.,Essen, L.O.,Wenzl, G.,Kim, Y.M.,Flecker, P. (deposition date: 2001-10-29, release date: 2001-11-16, Last modification date: 2024-10-30) |
| Primary citation | Voss, R.H.,Ermler, U.,Essen, L.O.,Wenzl, G.,Kim, Y.M.,Flecker, P. Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation. Eur.J.Biochem., 242:122-131, 1996 Cited by PubMed Abstract: The Bowman-Birk inhibitor from soybean is a small protein that contains a binary arrangement of trypsin-reactive and chymotrypsin-reactive subdomains. In this report, the crystal structure of this anticarcinogenic protein has been determined to 0.28-nm resolution by molecular replacement from crystals grown at neutral pH. The crystal structure differs from a previously determined NMR structure [Werner, M. H. & Wemmer, D. E. (1992) Biochemistry 31, 999-1010] in the relative orientation of the two enzyme-insertion loops, in some details of the main chain trace, in the presence of favourable contacts in the trypsin-insertion loop, and in the orientation of several amino acid side chains. The proximity of Met27 and Gln48 in the X-ray structure contradicts the solution structure, in which these two side chains point away from each other. The significant effect of a Met27-->Ile replacement on the inhibitory activity of the chymotrypsin-reactive subdomain agrees with the X-ray structure. Exposed hydrophobic patches, the presence of charged amino acid residues, and the presence of water molecules in the protein interior are in contrast to standard proteins that comprise a hydrophobic core and exposed polar amino acids. PubMed: 8954162DOI: 10.1111/j.1432-1033.1996.0122r.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
Download full validation report
