Cellobiohydrolase: Difference between revisions

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**[[1gpi]] - PcCBHI catalytic domain – ''Phanerochaete chrysosporium''<BR />
**[[1gpi]] - PcCBHI catalytic domain – ''Phanerochaete chrysosporium''<BR />
**[[1q9h]], [[3pfj]] - TeCBHI catalytic domain – ''Talaromyces emersonii''<BR />
**[[1q9h]], [[3pfj]] - TeCBHI catalytic domain – ''Talaromyces emersonii''<BR />
**[[2y9l]], [[2y9n]] - CBHI catalytic domain – ''Hypocrea lixii''
**[[2yok]], [[2y9n]] - CBHI catalytic domain – ''Hypocrea lixii''


*''Cellobiohydrolase I binary complex''
*''Cellobiohydrolase I binary complex''

Revision as of 13:57, 14 November 2016


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]

Structural highlights

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

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 14-November-2016

    • 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
  • 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
  • Cellobiohydrolase II
    • 3cbh – HjCBHII core
    • 1cb2 – HjCBHII catalytic domain (mutant)
    • 1hgw, 1hgy, 1oc6 – HjCBHII catalytic domain (mutant)
  • 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
  • Other cellobiohydrolases
    • 1l1y – CtCBH – Clostridium thermocellum
    • 1rq5 - CtCBH (mutant)
    • 1ut9 - CtCBH catalytic domain
    • 1sqj - GeCBH – Geotrichum
    • 3a64, 3vog - CcCBH catalytic domain - Coprinopsis cinerea
    • 3vof, 3voj - CcCBHI catalytic domain (mutant)
    • 4v1z – AfCBH 7A – Aspergillus fumigatus
  • Other cellobiohydrolases binary complex
    • 1l2a - CtCBH + glucose
    • 2ebs – GeCBH (mutant) + heptasaccharide
    • 3a9b, 3voh - CcCBHI catalytic domain + cellobiose
    • 3abx, 3voi - CcCBHI catalytic domain + cellotriose
    • 4v20 - AfCBH 7A + disaccharide

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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Michal Harel, Alexander Berchansky, Karsten Theis