5i79

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Crystal structure of a beta-1,4-endoglucanase mutant from Aspergillus niger in complex with sugar

Structural highlights

5i79 is a 2 chain structure with sequence from Aspergillus niger. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.35Å
Ligands:BGC, CA, NAG, PGE, PRD_900011
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EGLB_ASPNG Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates.[1]

Publication Abstract from PubMed

Eukaryotic 1,4-beta-endoglucanases (EC 3.2.1.4) have shown great potentials in many commercial applications because they effectively catalyze hydrolysis of cellulose, the main component of the plant cell wall. Here we expressed a glycoside hydrolase family (GH) 5 1,4-beta-endoglucanase from Aspergillus niger (AnCel5A) in Pichia pastoris, which exhibits outstanding pH and heat stability. In order to further investigate the molecular mechanism of AnCel5A, apo-form and cellotetraose (CTT) complex enzyme crystal structures were solved to high resolution. AnCel5A folds into a typical (beta/alpha)8-TIM barrel architecture, resembling other GH5 members. In the substrate binding cavity, CTT is found to bind to -4 - -1 subsites, and several polyethylene glycol molecules are found in positive subsites. In addition, several unique N-glycosylation motifs that may contribute to protein higher stability were observed from crystal structures. These results are of great importance for understanding the molecular mechanism of AnCel5A, and also provide guidance for further applications of the enzyme.

Functional and structural analysis of Pichia pastoris-expressed Aspergillus niger 1,4-beta-endoglucanase.,Yan J, Liu W, Li Y, Lai HL, Zheng Y, Huang JW, Chen CC, Chen Y, Jin J, Li H, Guo RT Biochem Biophys Res Commun. 2016 Jun 17;475(1):8-12. doi:, 10.1016/j.bbrc.2016.05.012. Epub 2016 May 3. PMID:27154222[2]

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

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See Also

References

  1. ↑ Hong J, Tamaki H, Akiba S, Yamamoto K, Kumagai H. Cloning of a gene encoding a highly stable endo-beta-1,4-glucanase from Aspergillus niger and its expression in yeast. J Biosci Bioeng. 2001;92(5):434-41. PMID:16233124 doi:10.1263/jbb.92.434
  2. ↑ Yan J, Liu W, Li Y, Lai HL, Zheng Y, Huang JW, Chen CC, Chen Y, Jin J, Li H, Guo RT. Functional and structural analysis of Pichia pastoris-expressed Aspergillus niger 1,4-beta-endoglucanase. Biochem Biophys Res Commun. 2016 Jun 17;475(1):8-12. doi:, 10.1016/j.bbrc.2016.05.012. Epub 2016 May 3. PMID:27154222 doi:http://dx.doi.org/10.1016/j.bbrc.2016.05.012

Contents


PDB ID 5i79

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