PDBsum entry 6y0h

Hydrolase

PDB id: 6y0h

Contents

Protein chain

189 a.a.

Waters ×282

PDB id:

6y0h

Name:

Hydrolase

Title:

High resolution structure of gh11 xylanase from nectria haematococca

Structure:

Endo-1,4-beta-xylanase. Chain: a. Engineered: yes. Other_details: endo-1,4-beta-xylanase activity

Source:

[Nectria] haematococca mpvi 77-13-4. Organism_taxid: 660122. Gene: nechadraft_106153. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008

Resolution:

1.00Å R-factor: 0.142 R-free: 0.154

Authors:

H.Andaleeb,C.Betzel,M.Perbandt,H.Brognaro

Key ref:

H.Andaleeb et al. (2020). High-resolution crystal structure and biochemical characterization of a GH11 endoxylanase from Nectria haematococca. Sci Rep, 10, 15658. PubMed id: 32973265 DOI: 10.1038/s41598-020-72644-w

Date:

07-Feb-20 Release date: 14-Oct-20

Protein chain

C7YSL3  (C7YSL3_NECH7) -  Endo-1,4-beta-xylanase from Fusarium vanettenii (strain ATCC MYA-4622 / CBS 123669 / FGSC 9596 / NRRL 45880 / 77-13-4)

Seq: 222 a.a.

Struc: 189 a.a.*

* PDB and UniProt seqs differ at 3 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.3.2.1.8 - endo-1,4-beta-xylanase.
• Reaction: Endohydrolysis of 1,4-beta-D-xylosidic linkages in xylans.

DOI no: 10.1038/s41598-020-72644-w

Sci Rep 10:15658 (2020)

PubMed id: 32973265

High-resolution crystal structure and biochemical characterization of a GH11 endoxylanase from Nectria haematococca.

H.Andaleeb, N.Ullah, S.Falke, M.Perbandt, H.Brognaro, C.Betzel.

ABSTRACT

Enzymatic degradation of vegetal biomass offers versatile procedures to improve the production of alternative fuels and other biomass-based products. Here we present the three-dimensional structure of a xylanase from Nectria haematococca (NhGH11) at 1.0 Å resolution and its functional properties. The atomic resolution structure provides details and insights about the complex hydrogen bonding network of the active site region and allowed a detailed comparison with homologous structures. Complementary biochemical studies showed that the xylanase can catalyze the hydrolysis of complex xylan into simple xylose aldopentose subunits of different lengths. NhGH11 can catalyze the efficient breakdown of beechwood xylan, xylan polysaccharide, and wheat arabinoxylan with turnover numbers of 1730.6 ± 318.1 min^-1, 1648.2 ± 249.3 min^-1 and 2410.8 ± 517.5 min^-1 respectively. NhGH11 showed maximum catalytic activity at pH 6.0 and 45 °C. The mesophilic character of NhGH11 can be explained by distinct structural features in comparison to thermophilic GH11 enzymes, including the number of hydrogen bonds, side chain interactions and number of buried water molecules. The enzymatic activity of NhGH11 is not very sensitive to metal ions and chemical reagents that are typically present in associated industrial production processes. The data we present highlights the potential of NhGH11 to be applied in industrial biomass degradation processes.