In molecular biology, the chitinase A N-terminal domain is found at the N-terminus of a number of bacterial chitinases and similar viral proteins. It is organised into a fibronectin III module domain-like fold, comprising only beta strands. Its function is not known, but it may be involved in interaction with the enzyme substrate, chitin.[1][2] It is separated by a hinge region from the catalytic domain; this hinge region is probably mobile, allowing the N-terminal domain to have different relative positions in solution.[1]
ChitinaseA_N | |||||||||
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Identifiers | |||||||||
Symbol | ChitinaseA_N | ||||||||
Pfam | PF08329 | ||||||||
Pfam clan | CL0159 | ||||||||
InterPro | IPR013540 | ||||||||
SCOP2 | 1ctn / SCOPe / SUPFAM | ||||||||
CDD | cd02848 | ||||||||
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References
edit- ^ a b Perrakis A, Tews I, Dauter Z, Oppenheim AB, Chet I, Wilson KS, Vorgias CE (December 1994). "Crystal structure of a bacterial chitinase at 2.3 A resolution". Structure. 2 (12): 1169–80. doi:10.1016/s0969-2126(94)00119-7. PMID 7704527.
- ^ Perrakis A, Ouzounis C, Wilson KS (1997). "Evolution of immunoglobulin-like modules in chitinases: their structural flexibility and functional implications". Fold Des. 2 (5): 291–4. doi:10.1016/s1359-0278(97)00040-0. PMID 9377712.