Structure of a Fibronectin Type III-Like Module from Clostridium Thermocellum

Markus Alahuhta, Qi Xu, Roman Brunecky, William S. Adney, Shi You Ding, Michael E. Himmel, Vladimir V. Lunin

Research output: Contribution to journalArticlepeer-review

12 Scopus Citations

Abstract

The 1.6 Å resolution structure of a fibronectin type III-like module from Clostridium thermocellum (PDB code 3mpc) with two molecules in the asymmetric unit is reported. The crystals used for data collection belonged to space group P212121, with unit-cell parameters a = 35.43, b = 45.73, c = 107.72 Å, and the structure was refined to an R factor of 0.166. Structural comparisons found over 800 similar structures in the Protein Data Bank. The broad range of different proteins or protein domains with high structural similarity makes it especially demanding to classify these proteins. Previous studies of fibronectin type III-like modules have indicated that they might function as ligand-binding modules, as a compact form of peptide linkers or spacers between other domains, as cellulose-disrupting modules or as proteins that help large enzyme complexes remain soluble.

Original languageAmerican English
Pages (from-to)878-880
Number of pages3
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number8
DOIs
StatePublished - 2010

NREL Publication Number

  • NREL/JA-270-48980

Keywords

  • fibronectin type III-like modules
  • X-domain
  • X-module

Fingerprint

Dive into the research topics of 'Structure of a Fibronectin Type III-Like Module from Clostridium Thermocellum'. Together they form a unique fingerprint.

Cite this