当前位置： SCI文献检索 > INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES期刊下所有文献 > Structure and dynamics analysis of a family 43 glycoside hydrolase α-L-arabinofuranosidase (PsGH43_12) from Pseudopedobacter saltans by computational modeling and small-angle X-ray scattering.

Structure and dynamics analysis of a family 43 glycoside hydrolase α-L-arabinofuranosidase (PsGH43_12) from Pseudopedobacter saltans by computational modeling and small-angle X-ray scattering.

Abstract：

:The structure and molecular dynamics of α-L-arabinofuranosidase (PsGH43_12) of family 43 glycoside hydrolase, subfamily 12 from Pseudopedobacter saltans were studied. The modeled PsGH43_12 structure displayed 5-bladed β-propeller fold at N-terminal and β-sandwich fold at C terminal. Ramachandran plot showed 95.7% residues in favored and 3.3% in the generously allowed region and only 1% residues in the disallowed region. The secondary structure analysis of PsGH43_12 by circular dichroism revealed 2.7% α-helices, 30.33% β-strands and 66.97% random coils. Protein melting study of PsGH43_12 showed complete unfolding at 65°C and did not require any metal ion for its stability. Molecular docking analysis confirmed the involvement of active site residues Asp71, Asp180 and Glu247 in the catalysis, which was also confirmed by the site-directed mutagenesis of these residues. SAXS analysis displayed that PsGH43_12 is monomeric and a fully folded state in solution form. Guinier analysis gave the radius of gyration (Rg) 2.8 ± 0.09 nm. The maximum dimension and Rg of PsGH43_12 estimated from P(R) plot were 9.7 nm and 2.81 nm, respectively. The ab initio derived dummy model of PsGH43_12 displayed a bell-like shape. The ab initio derived dummy model superposed well with its comparative modeled structure except the N-terminal His6-tag region.

journal_name

Int J Biol Macromol

journal_title

International journal of biological macromolecules

authors

Thakur A,Sharma K,Jaiswal K,Goyal A

doi

10.1016/j.ijbiomac.2020.07.007

subject

Has Abstract

pub_date

2020-11-15 00:00:00

pages

582-592

eissn

0141-8130

issn

1879-0003

pii

S0141-8130(20)33751-X

journal_volume

163

pub_type

杂志文章

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