Cellobiohydrolase
FunctionCellobiohydrolase (CBH) is a cellulase which degrades cellulose by hydrolysing the 1,4-β-D-glycosidic bonds. CBH is an exocellulase which cleaves two to four units from the ends of cellulose. There are two types of CBH. CBHI cleaves progressively from the reducing end while CBHII cleaves progressively from the nonreducing end of cellulose.[1] Structural highlightsThe of CBH contains (Gln-Asp-Glu in 3cel, cyan) and is situated at the .[2] |
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3D structures of cellobiohydrolase3D structures of cellobiohydrolase
Updated on 30-March-2017
- 1cel – HjCBHI core – Hypocrea jecorina
- 1cbh, 2cbh – HjCBHI C terminal – NMR
- 1azh, 1az6, 1azj, 1azk - HjCBHI cellulose-binding domain (mutant) - NMR
- 2cel, 4cel, 1egn, 1q2b - HjCBHI catalytic domain (mutant)
- 1gpi - PcCBHI catalytic domain – Phanerochaete chrysosporium
- 1q9h, 3pfj - TeCBHI catalytic domain – Talaromyces emersonii
- 2yok, 2y9n - CBHI catalytic domain – Hypocrea lixii
- 5mcc, 5mcd, 5mce, 5mcf, 5mch, 5mci, 5mcj, 5mck, 5mcl, 5mcm, 5mcn, 4xnn – wfCBHI – water flea
- 4zzv, 5amp - GcCBHI catalytic domain – Galactomyces candidum
- 1cel – HjCBHI core – Hypocrea jecorina
- Cellobiohydrolase I binary complex
- 3cel - HjCBHI catalytic domain (mutant) + cellobiose
- 5cel, 1q2e - HjCBHI catalytic domain (mutant) + cellotetraose
- 6cel - HjCBHI catalytic domain (mutant) + cellopentaose
- 7cel - HjCBHI catalytic domain (mutant) + glucose
- 2v3i, 2v3r - HjCBHI catalytic domain + phenanthrenolol
- 1dy4 - TrCBHI catalytic domain + propranolol – Trichoderma reesei
- 1h46 - PcCBHI catalytic domain + propranolol
- 1z3t - PcCBHI catalytic domain + cellobiose
- 1z3v - PcCBHI catalytic domain + lactose
- 1z3w - PcCBHI catalytic domain + cellobioimidazole
- 3pfx - TeCBHI catalytic domain + cellobiose
- 3pfz - TeCBHI catalytic domain + cellotetraose + cellobiose
- 3pl3 - TeCBHI catalytic domain + cellopentaose
- 4zzu - GgCBHI catalytic domain + cellotetraose – Galactomyces geotrichum
- 4zzw - GgCBHI catalytic domain + cellobiose
- 4zzt - GcCBHI catalytic domain + cellotraiose
- 3cel - HjCBHI catalytic domain (mutant) + cellobiose
- Cellobiohydrolase II
- Cellobiohydrolase II binary complex
- 1bvw - HiCBHII catalytic domain + mannose – Humicola insolens
- 2bvw - HiCBHII catalytic domain + glucose + cellotetraose
- 1gz1, 1oc5 - HiCBHII catalytic domain (mutant) + cellotetraose
- 1oc7 - HiCBHII catalytic domain (mutant) + cellopentaose
- 1ocj - HiCBHII catalytic domain + cellopentaose
- 1ocb - HiCBHII catalytic domain + fluorescent substrate
- 1ocn - HiCBHII catalytic domain (mutant) + isofagomine
- 1qjw - TrCBHII catalytic domain (mutant) + cellotetraose
- 1qk0 - TrCBHII catalytic domain + polysaccharide
- 1qk2 - TrCBHII catalytic domain + cellotetraose
- 1bvw - HiCBHII catalytic domain + mannose – Humicola insolens
- Other cellobiohydrolases
- Other cellobiohydrolases binary complex
ReferencesReferences
- ↑ Divne C, Stahlberg J, Teeri TT, Jones TA. High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei. J Mol Biol. 1998 Jan 16;275(2):309-25. PMID:9466911 doi:http://dx.doi.org/10.1006/jmbi.1997.1437
- ↑ Stahlberg J, Divne C, Koivula A, Piens K, Claeyssens M, Teeri TT, Jones TA. Activity studies and crystal structures of catalytically deficient mutants of cellobiohydrolase I from Trichoderma reesei. J Mol Biol. 1996 Nov 29;264(2):337-49. PMID:8951380 doi:http://dx.doi.org/10.1006/jmbi.1996.0644