2NLR
STREPTOMYCES LIVIDANS ENDOGLUCANASE (EC: 3.2.1.4) COMPLEX WITH MODIFIED GLUCOSE TRIMER
Summary for 2NLR
| Entry DOI | 10.2210/pdb2nlr/pdb |
| Descriptor | PROTEIN (ENDOGLUCANASE (E.C.3.2.1.4)), beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-2-deoxy-2-fluoro-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | hydrolase (endoglucanase), glycosyl hydrolase, family 12, endoglucanase, celb2, glycosyl-enzyme intermediate, hydrolase |
| Biological source | Streptomyces lividans |
| Total number of polymer chains | 1 |
| Total formula weight | 25085.14 |
| Authors | Sulzenbacher, G.,Dupont, C.,Davies, G.J. (deposition date: 1998-11-02, release date: 1999-11-10, Last modification date: 2024-10-30) |
| Primary citation | Sulzenbacher, G.,Mackenzie, L.F.,Wilson, K.S.,Withers, S.G.,Dupont, C.,Davies, G.J. The crystal structure of a 2-fluorocellotriosyl complex of the Streptomyces lividans endoglucanase CelB2 at 1.2 A resolution. Biochemistry, 38:4826-4833, 1999 Cited by PubMed Abstract: Glycoside hydrolases have been classified into over 66 families on the basis of amino acid sequence. Recently a number of these families have been grouped into "clans" which share a common fold and catalytic mechanism [Henrissat, B., and Bairoch, A. (1996) Biochem. J. 316, 695-696]. Glycoside hydrolase Clan GH-C groups family 11 xylanases and family 12 cellulases, which share the same jellyroll topology, with two predominantly antiparallel beta-sheets forming a long substrate-binding cleft, and act with net retention of anomeric configuration. Here we present the three-dimensional structure of a family 12 endoglucanase, Streptomyces lividans CelB2, in complex with a 2-deoxy-2-fluorocellotrioside. Atomic resolution (1.2 A) data allow clear identification of two distinct species in the crystal. One is the glycosyl-enzyme intermediate, with the mechanism-based inhibitor covalently linked to the nucleophile Glu 120, and the other a complex with the reaction product, 2-deoxy-2-fluoro-beta-D-cellotriose. The active site architecture of the complex provides insight into the double-displacement mechanism of retaining glycoside hydrolases and also sheds light on the basis of the differences in specificity between family 12 cellulases and family 11 xylanases. PubMed: 10200171DOI: 10.1021/bi982648i PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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