Structural Studies of a Two-domain Chitinase from Streptomyces griseus HUT6037

Kezuka, Yuichiro; Ohishi, Manabu; Itoh, Yoshifumi; Watanabe, Jun; Mitsutomi, Masaru; Watanabe, Takeshi; Nonaka, Takamasa

doi:10.1016/j.jmb.2006.02.013

Cited by 87 publications

(94 citation statements)

References 53 publications

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“…Two of these (residues 112-114 and 118-120) have been observed previously [3]. Three similar β strands have also been identified in the structurally related chitinase isolated from Streptomyces griseus that also belongs to family 19 chitinases [46], leading to a β-sheet content of around 7% in both chitinases, and thus far less than the 15-23% predicted here. The lack of regular hydrogen-bonding patterns in these short β-sheet segments prevents their detection by conventional secondary structure assignment programs, like DSSP [47].…”

Section: Structural Characterization Of Papaya Chitinasessupporting

confidence: 80%

Structural characterization of two papaya chitinases, a family GH19 of glycosyl hydrolases

Huet

Wyckmans

Wintjens

et al. 2006

Cell. Mol. Life Sci.

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Two chitinases, able to use tetra-N-acetylglucosamine, chitin and chitosan as substrates, were characterized after purification from Carica papaya latex. The complete amino acid sequence of the major form and about 40% of the minor one were determined through proteolytic digestions and mass spectroscopy analysis. Sequencing demonstrated that both papaya chitinases are members of the family 19 of glycosyl hydrolases (GH19). Based on the known 3-D structures of other members of family GH19, it was expected that papaya chitinases would adopt all-alpha structures. However, circular dichroism and infrared spectroscopy indicated, for the papaya chitinases, a content of 15-20% of extended structures besides the expected 40% of alpha helices. Since the fully sequenced papaya chitinase contains a large number of proline residues the possibility that papaya chitinase contains polyproline II stretches was examined in the context of their resistance against proteolytic degradation.

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Section: Structural Characterization Of Papaya Chitinasessupporting

confidence: 80%

Structural characterization of two papaya chitinases, a family GH19 of glycosyl hydrolases

Huet

Wyckmans

Wintjens

et al. 2006

Cell. Mol. Life Sci.

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“…On the other hand, a GH19 chitinase lacking the loops except Loop III (''loopless'' chitinases) was isolated from moss, Bryum coronatum [11]. Based on the amino acid sequence alignment, the structure of the moss enzyme is closely related to those of GH19 chitinases from Streptomyces griseus HUT6037 [12], Streptomyces coelicolor A3(2) [13], and Norway spruce [14]. Thus, the structural organization of the GH19 enzymes was intensively studied, and the structural data have been accumulated.…”

Section: Introductionmentioning

confidence: 99%

Complete subsite mapping of a “loopful” GH19 chitinase from rye seeds based on its crystal structure

et al. 2013

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Edited by Richard Cogdell Keywords:Crystal structure GH19 chitinase Rye seed Chitin oligosaccharide Domain motion a b s t r a c t Crystallographic analysis of a mutated form of ''loopful'' GH19 chitinase from rye seeds a double mutant RSC-c, in which Glu67 and Trp72 are mutated to glutamine and alanine, respectively, (RSC-c-E67Q/W72A) in complex with chitin tetrasaccharide (GlcNAc) 4 revealed that the entire substrate-binding cleft was completely occupied with the sugar residues of two (GlcNAc) 4 molecules. One (GlcNAc) 4 molecule bound to subsites À4 to À1, while the other bound to subsites +1 to +4. Comparisons of the main chain conformation between liganded RSC-c-E67Q/W72A and unliganded wild type RSC-c suggested domain motion essential for catalysis. This is the first report on the complete subsite mapping of GH19 chitinase.

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“…The last differs from typical class I enzymes in that it possesses two CtBMs rather than one; however, the CM has 55-60% amino acid sequence identity to enzymes of class I and II. Family 19 bacterial chitinase structures have been presented for chitinase C from Streptomyces griseus HUT6037 (PDB entries 1WVU, 1WVV and 2DBT (Kezuka et al 2006)) and chitinase G from Streptomyces coelicolor A3(2) (PDB entry 2CJL (Hoell et al 2006)). …”

Section: Introductionmentioning

confidence: 99%

The first crystal structures of a family 19 class IV chitinase: the enzyme from Norway spruce

Ubhayasekera

Rawat

et al. 2009

Plant Mol Biol

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Chitinases help plants defend themselves against fungal attack, and play roles in other processes, including development. The catalytic modules of most plant chitinases belong to glycoside hydrolase family 19. We report here x-ray structures of such a module from a Norway spruce enzyme, the first for any family 19 class IV chitinase. The bi-lobed structure has a wide cleft lined by conserved residues; the most interesting for catalysis are Glu113, the proton donor, and Glu122, believed to be a general base that activate a catalytic water molecule. Comparisons to class I and II enzymes show that loop deletions in the class IV proteins make the catalytic cleft shorter and wider; from modeling studies, it is predicted that only three N-acetylglucosamine-binding subsites exist in class IV. Further, the structural comparisons suggest that the family 19 enzymes become more closed on substrate binding. Attempts to solve the structure of the complete protein including the associated chitin-binding module failed, however, modeling studies based on close relatives indicate that the binding module recognizes at most three N-acetylglucosamine units. The combined results suggest that the class IV enzymes are optimized for shorter substrates than the class I and II enzymes, or alternatively, that they are better suited for action on substrates where only small regions of chitin chain are accessible. Intact spruce chitinase is shown to possess antifungal activity, which requires the binding module; removing this module had no effect on measured chitinase activity.

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Structural Studies of a Two-domain Chitinase from Streptomyces griseus HUT6037

Cited by 87 publications

References 53 publications

Structural characterization of two papaya chitinases, a family GH19 of glycosyl hydrolases

Structural characterization of two papaya chitinases, a family GH19 of glycosyl hydrolases

Complete subsite mapping of a “loopful” GH19 chitinase from rye seeds based on its crystal structure

The first crystal structures of a family 19 class IV chitinase: the enzyme from Norway spruce

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