Integrative structure determination reveals functional global flexibility for an ultra-multimodular arabinanase. Academic Article uri icon

Overview

abstract

  • AbnA is an extracellular GH43 α-L-arabinanase from Geobacillus stearothermophilus, a key bacterial enzyme in the degradation and utilization of arabinan. We present herein its full-length crystal structure, revealing the only ultra-multimodular architecture and the largest structure to be reported so far within the GH43 family. Additionally, the structure of AbnA appears to contain two domains belonging to new uncharacterized carbohydrate-binding module (CBM) families. Three crystallographic conformational states are determined for AbnA, and this conformational flexibility is thoroughly investigated further using the "integrative structure determination" approach, integrating molecular dynamics, metadynamics, normal mode analysis, small angle X-ray scattering, dynamic light scattering, cross-linking, and kinetic experiments to reveal large functional conformational changes for AbnA, involving up to ~100 Å movement in the relative positions of its domains. The integrative structure determination approach demonstrated here may apply also to the conformational study of other ultra-multimodular proteins of diverse functions and structures.

authors

  • Lansky, Shifra
  • Salama, Rachel
  • Biarnés, Xevi
  • Shwartstein, Omer
  • Schneidman-Duhovny, Dina
  • Planas, Antoni
  • Shoham, Yuval
  • Shoham, Gil

publication date

  • May 16, 2022

Research

keywords

  • Glycoside Hydrolases

Identity

PubMed Central ID

  • PMC9110388

Scopus Document Identifier

  • 85130193894

Digital Object Identifier (DOI)

  • 10.1016/0003-2697(92)90204-K

PubMed ID

  • 35577850

Additional Document Info

volume

  • 5

issue

  • 1