1RH9
Family GH5 endo-beta-mannanase from Lycopersicon esculentum (tomato)
Summary for 1RH9
| Entry DOI | 10.2210/pdb1rh9/pdb |
| Related | 1BQC 1QNP |
| Descriptor | endo-beta-mannanase (1 entity in total) |
| Functional Keywords | endo-beta-mannase, retaining, glycoside hydrolase family 5, mannan, hydrolase |
| Biological source | Solanum lycopersicum |
| Total number of polymer chains | 1 |
| Total formula weight | 42435.91 |
| Authors | Oakley, A.J.,Bourgault, R.,Bewley, J.D.,Wilce, M.C.J. (deposition date: 2003-11-14, release date: 2005-04-19, Last modification date: 2024-10-30) |
| Primary citation | Bourgault, R.,Oakley, A.J.,Bewley, J.D.,Wilce, M.C. Three-dimensional structure of (1,4)-beta-D-mannan mannanohydrolase from tomato fruit. Protein Sci., 14:1233-1241, 2005 Cited by PubMed Abstract: The three-dimensional crystal structure of tomato (Lycopersicon esculentum) beta-mannanase 4a (LeMAN4a) has been determined to 1.5 A resolution. The enzyme adopts the (beta/alpha)(8) fold common to the members of glycohydrolase family GH5. The structure is comparable with those of the homologous Trichoderma reesei and Thermomonospora fusca beta-mannanases: There is a conserved three-stranded beta-sheet located near the N terminus that stacks against the central beta-barrel at the end opposite the active site. Three noncanonical beta-helices surround the active site. Similar helices are found in T. reesei but not T. fusca beta-mannanase. By analogy with other beta-mannanases, the catalytic acid/base residue is E204 and the nucleophile residue is E318. The active site cleft of L. esculentum beta-mannanase most closely resembles that of the T. reesei isozyme. A model of substrate binding in LeMAN4a is proposed in which the mannosyl residue occupying the -1 subsite of the enzyme adopts the (1)S(5) skew-boat conformation. PubMed: 15840830DOI: 10.1110/ps.041260905 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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