Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The 1.6 A 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 P2(1)2(1)2(1), with unit-cell parameters a=35.43, b=45.73, c=107.72 A, 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.
Structure of a fibronectin type III-like module from Clostridium thermocellum.,Alahuhta M, Xu Q, Brunecky R, Adney WS, Ding SY, Himmel ME, Lunin VV Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Aug 1;66(Pt, 8):878-80. Epub 2010 Jul 27. PMID:20693658[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Alahuhta M, Xu Q, Brunecky R, Adney WS, Ding SY, Himmel ME, Lunin VV. Structure of a fibronectin type III-like module from Clostridium thermocellum. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Aug 1;66(Pt, 8):878-80. Epub 2010 Jul 27. PMID:20693658 doi:10.1107/S1744309110022529
