1XVO
Trypsin from Fusarium oxysporum at pH 6
Summary for 1XVO
Entry DOI | 10.2210/pdb1xvo/pdb |
Related | 1PPZ 1PQ5 1PQ8 1PQA 1XVM |
Descriptor | trypsin, SULFATE ION (3 entities in total) |
Functional Keywords | trypsin, atomic resolution, hydrolase |
Biological source | Fusarium oxysporum |
Cellular location | Secreted: P35049 |
Total number of polymer chains | 1 |
Total formula weight | 22584.74 |
Authors | Schmidt, A.,Lamzin, V.S. (deposition date: 2004-10-28, release date: 2005-07-26, Last modification date: 2024-11-13) |
Primary citation | Schmidt, A.,Lamzin, V.S. Extraction of functional motion in trypsin crystal structures. Acta Crystallogr.,Sect.D, 61:1132-1139, 2005 Cited by PubMed Abstract: The analysis of anisotropic atomic displacement parameters for the direct extraction of functionally relevant motion from X-ray crystal structures of Fusarium oxysporum trypsin is presented. Several atomic resolution structures complexed with inhibitors or substrates and determined at different pH values and temperatures were investigated. The analysis revealed a breathing-like molecular motion conserved across trypsin structures from two organisms and three different crystal forms. Directional motion was observed suggesting a change of the width of the substrate-binding cleft and a change in the length of the specificity pocket. The differences in direction of motion across the structures are dependent on the mode of substrate or inhibitor binding and the chemical environment around the active-site residues. Together with the occurrence of multiple-residue conformers, they reflect spatial rearrangement throughout the deacylation pathway. PubMed: 16041079DOI: 10.1107/S0907444905016732 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (0.84 Å) |
Structure validation
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