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431 a.a.
_CA
_ZN
_NI
Key reference
DOI no: 10.1021/bi025816m Biochemistry 41:11134-11142 (2002) PubMed id: 12220178
Crystal structure of the cellulase Cel9M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases. G.Parsiegla, A.Belaïch, J.P.Belaïch, R.Haser. ABSTRACT
Cellulases cleave the beta-1.4 glycosidic bond of cellulose. They have been characterized as endo or exo and processive or nonprocessive cellulases according to their action mode on the substrate. Different types of these cellulases may coexist in the same glycoside hydrolase family, which have been classified according to their sequence homology and catalytic mechanism. The bacterium C. celluloyticum produces a set of different cellulases who belong mostly to glycoside hydrolase families 5 and 9. As an adaptation of the organism to different macroscopic substrates organizations and to maximize its cooperative digestion, it is expected that cellulases of these families are active on the various macroscopic organizations of cellulose chains. The nonprocessive cellulase Cel9M is the shortest variant of family 9 cellulases (subgroup 9(C)) which contains only the catalytic module to interact with the substrate. The crystal structures of free native Cel9M and its complex with cellobiose have been solved to 1.8 and 2.0 A resolution, respectively. Other structurally known family 9 cellulases are the nonprocessive endo-cellulase Cel9D from C. thermocellum and the processive endo-cellulase Cel9A from T. fusca, from subgroups 9(B1) and 9(A), respectively, whose catalytic modules are fused to a second domain. These enzymes differ in their activity on substrates with specific macroscopic appearances. The comparison of the catalytic module of Cel9M with the two other known GH family 9 structures may give clues to explain its substrate profile and action mode.
Literature references that cite this PDB file's key reference
PubMed id Reference
19622857 J.H.Pereira, R.Sapra, J.V.Volponi, C.L.Kozina, B.Simmons, and P.D.Adams (2009).
Structure of endoglucanase Cel9A from the thermoacidophilic Alicyclobacillus acidocaldarius.Acta Crystallogr D Biol Crystallogr, 65, 744-750.
PDB code: 3ez8
18663584 L.C.Tsai, Y.N.Chen, and L.F.Shyur (2008).
Structural modeling of glucanase-substrate complexes suggests a conserved tyrosine is involved in carbohydrate recognition in plant 1,3-1,4-beta-D-glucanases.J Comput Aided Mol Des, 22, 915-923.
17022659 M.Desvaux (2006).
Unravelling carbon metabolism in anaerobic cellulolytic bacteria.Biotechnol Prog, 22, 1229-1238.
16102601 M.Desvaux (2005).
Clostridium cellulolyticum: model organism of mesophilic cellulolytic clostridia.FEMS Microbiol Rev, 29, 741-764.
15604820 L.Hildén, and G.Johansson (2004).
Recent developments on cellulases and carbohydrate-binding modules with cellulose affinity.Biotechnol Lett, 26, 1683-1693.
15148314 T.Itoh, S.Akao, W.Hashimoto, B.Mikami, and K.Murata (2004).
Crystal structure of unsaturated glucuronyl hydrolase, responsible for the degradation of glycosaminoglycan, from Bacillus sp. GL1 at 1.8 A resolution.J Biol Chem, 279, 31804-31812.
PDB code: 1vd5 The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.
