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5h4u

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Crystal structure of cellulase from Antarctic springtail, Cryptopygus antarcticus

Structural highlights

5h4u is a 3 chain structure with sequence from Cryptopygus antarcticus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.6Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GUN_CRYAT Hydrolyzes carboxymethylcellulose (CMC) (PubMed:24848382, PubMed:28156112). Hydrolyzes also lichenan and barley beta-1,4-D-glucan. CMC is hydrolyzed majorily to cellobiose (G2), cellotriose (G3) and cellotetraose (G4). Cellohexaose (G6) is hydrolyzed to G4 and G2 with traces of G3. Cellopentaose (G5) is completely hydrolyzed to G2 and G3, and G4 is partially hydrolyzed to G2. Does not hydrolyze G2 or G3. Does not hydrolyze crystalline cellulose, soluble starch, xylan, mannan or laminarin (PubMed:28156112).^[1] ^[2]

Publication Abstract from PubMed

The CaCel gene from Antarctic springtail Cryptopygus antarcticus codes for a cellulase belonging to the glycosyl hydrolase family 45 (GHF45). Phylogenetic, biochemical, and structural analyses revealed that the CaCel gene product (CaCel) is closely related to fungal GHF45 endo-beta-1,4-glucanases. The organization of five introns within the open reading frame of the CaCel gene indicates its endogenous origin in the genome of the species, which suggests the horizontal transfer of the gene from fungi to the springtail. CaCel exhibited optimal activity at pH 3.5, retained 80% of its activity at 0-10 degrees C, and maintained a half-life of 4 h at 70 degrees C. Based on the structural comparison between CaCel and a fungal homologue, we deduced the structural basis for the unusual characteristics of CaCel. Under acidic conditions at 50 degrees C, CaCel was effective to digest the green algae (Ulva pertusa), suggesting that it could be exploited for biofuel production from seaweeds.

Genetic and Structural Characterization of a Thermo-Tolerant, Cold-Active, and Acidic Endo-beta-1,4-glucanase from Antarctic Springtail, Cryptopygus antarcticus.,Song JM, Hong SK, An YJ, Kang MH, Hong KH, Lee YH, Cha SS J Agric Food Chem. 2017 Mar 1;65(8):1630-1640. doi: 10.1021/acs.jafc.6b05037., Epub 2017 Feb 16. PMID:28156112^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hong SM, Sung HS, Kang MH, Kim CG, Lee YH, Kim DJ, Lee JM, Kusakabe T. Characterization of Cryptopygus antarcticus endo-β-1,4-glucanase from Bombyx mori expression systems. Mol Biotechnol. 2014 Oct;56(10):878-89. PMID:24848382 doi:10.1007/s12033-014-9767-8
↑ Song JM, Hong SK, An YJ, Kang MH, Hong KH, Lee YH, Cha SS. Genetic and Structural Characterization of a Thermo-Tolerant, Cold-Active, and Acidic Endo-beta-1,4-glucanase from Antarctic Springtail, Cryptopygus antarcticus. J Agric Food Chem. 2017 Mar 1;65(8):1630-1640. doi: 10.1021/acs.jafc.6b05037., Epub 2017 Feb 16. PMID:28156112 doi:http://dx.doi.org/10.1021/acs.jafc.6b05037
↑ Song JM, Hong SK, An YJ, Kang MH, Hong KH, Lee YH, Cha SS. Genetic and Structural Characterization of a Thermo-Tolerant, Cold-Active, and Acidic Endo-beta-1,4-glucanase from Antarctic Springtail, Cryptopygus antarcticus. J Agric Food Chem. 2017 Mar 1;65(8):1630-1640. doi: 10.1021/acs.jafc.6b05037., Epub 2017 Feb 16. PMID:28156112 doi:http://dx.doi.org/10.1021/acs.jafc.6b05037