Cellobiohydrolase

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Function

Cellobiohydrolase (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]. The exo-acting CBH I is called Cel7A. The endo-acting CBH I is called Cel7B.

Structural highlights

The of CBH contains (Gln-Asp-Glu in 3cel, cyan) and is situated at the .[2] Water molecules shown as red spheres.

Glycosylated cellobiohydrolase I catalytic domain complex with cellobiose and Cd+2 ions (yellow) (PDB code 3cel)

Drag the structure with the mouse to rotate

3D structures of cellobiohydrolase3D structures of cellobiohydrolase

Updated on 09-April-2018

  • Cellobiohydrolase I binary complex
    • 3cel, 4uwt - HjCBHI Cel7A catalytic domain (mutant) + cellobiose
    • 5cel, 1q2e, 4d5v - HjCBHI Cel7A catalytic domain (mutant) + cellotetraose
    • 4d5q - HjCBHI Cel7A catalytic domain + cellopentaose
    • 6cel, 4d5o, 4d5p - HjCBHI Cel7A catalytic domain (mutant) + cellopentaose
    • 7cel - HjCBHI catalytic domain (mutant) + glucose
    • 2v3i, 2v3r - HjCBHI Cel7A catalytic domain + phenanthrenolol
    • 1dy4 - TrCBHI Cel7A catalytic domain + propranolol
    • 4c4c - TrCBHI Cel7A catalytic domain (mutant) + cellononaose
    • 4c4d, 4d5i, 4d5j - TrCBHI Cel7A catalytic domain (mutant) + cellotrioside
    • 1h46 - PcCBHI Cel7D catalytic domain + propranolol
    • 1z3t - PcCBHI Cel7D catalytic domain + cellobiose
    • 1z3v - PcCBHI Cel7D catalytic domain + lactose
    • 1z3w - PcCBHI Cel7D catalytic domain + cellobioimidazole
    • 3pfx - TeCBHI Cel7A catalytic domain + cellobiose
    • 3pfz - TeCBHI Cel7A catalytic domain + cellotetraose + cellobiose
    • 3pl3 - TeCBHI Cel7A catalytic domain + cellopentaose
    • 4zzu - GgCBHI Cel7A catalytic domain + cellotetraose – Galactomyces geotrichum
    • 4zzw - GgCBHI Cel7A catalytic domain + cellobiose
    • 4zzt - GcCBHI Cel7A catalytic domain + cellotraiose
  • Cellobiohydrolase II or Cellobiohydrolase Cel6A or exoglucanase 2
    • 3cbh – HjCBHII core
    • 1cb2 – HjCBHII catalytic domain (mutant)
    • 1hgw, 1hgy, 1oc6 – HjCBHII Cel6A catalytic domain (mutant)
  • Cellobiohydrolase II complex
    • 1bvw - HiCBHII catalytic domain + mannose – Humicola insolens
    • 4au0 - HjCBHII catalytic domain Cel6A (mutant) + cellobioside
    • 2bvw - HiCBHII Cel6A catalytic domain + glucose + cellotetraose
    • 1gz1, 1oc5 - HiCBHII Cel6A catalytic domain (mutant) + cellotetraose
    • 1oc7 - HiCBHII Cel6A catalytic domain (mutant) + cellopentaose
    • 1ocj - HiCBHII Cel6A catalytic domain + cellopentaose
    • 1ocb - HiCBHII Cel6A catalytic domain + fluorescent substrate
    • 1ocn - HiCBHII Cel6A catalytic domain (mutant) + isofagomine
    • 1qjw - TrCBHII Cel6A catalytic domain (mutant) + cellotetraose
    • 4ax6, 4ax7 - TrCBHII Cel6A catalytic domain (mutant) + cellobioside
    • 1qk0 - TrCBHII Cel6A catalytic domain + polysaccharide
    • 1qk2 - TrCBHII Cel6A catalytic domain + cellotetraose
  • Other cellobiohydrolases
    • 1l1y – CtCBH CelS – Clostridium thermocellum
    • 1rq5 - CtCBHA (mutant)
    • 1ut9 - CtCBHA catalytic domain
    • 1sqj - GgCBH
    • 3a64, 3vog - CcCBH Cel6C catalytic domain - Coprinopsis cinerea
    • 3vof, 3voj - CcCBHI Cel6C catalytic domain (mutant)
    • 4v1z – AfCBH Cel7A – Aspergillus fumigatus
    • 2mte – CBH CelS residues 673-741 – Ruminiclostridium thermocellum - NMR
  • Other cellobiohydrolases binary complex
    • 1l2a - CtCBH CelS + glucose
    • 2ebs – GgCBH (mutant) + heptasaccharide
    • 3a9b, 3voh - CcCBHI Cel6C catalytic domain + cellobiose
    • 3abx, 3voi - CcCBHI Cel6C catalytic domain + cellotriose
    • 4v20 - AfCBH Cel7A + disaccharide
    • 4v0z - TrCBH Cel7A + cellobiose
    • 4vwt - TrCBH Cel7A (mutant) + cellobiose

ReferencesReferences

  1. 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
  2. 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

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