1K85

Solution structure of the fibronectin type III domain from Bacillus circulans WL-12 Chitinase A1.

Summary for 1K85

• Entry DOI: 10.2210/pdb1k85/pdb
• NMR Information: BMRB: 5178
• Descriptor: CHITINASE A1 (1 entity in total)
• Functional Keywords: fibronectin type iii domain, chitinase, chitin binding domain, carbohydrase, horizontal gene transfer, hydrolase
• Biological source: Bacillus circulans
• Total number of polymer chains: 1
• Total formula weight: 8695.43

Authors

Jee, J.G.,Ikegami, T.,Hashimoto, M.,Kawabata, T.,Ikeguchi, M.,Watanabe, T.,Shirakawa, M. (deposition date: 2001-10-23, release date: 2002-12-18, Last modification date: 2024-05-29)

Primary citation

Jee, J.G.,Ikegami, T.,Hashimoto, M.,Kawabata, T.,Ikeguchi, M.,Watanabe, T.,Shirakawa, M.
Solution Structure of the Fibronectin Type III Domain from Bacillus circulans WL-12 Chitinase A1
J.Biol.Chem., 277:1388-1397, 2002

PubMed Abstract: Growing evidence suggests that horizontal gene transfer plays an integral role in the evolution of bacterial genomes. One of the debated examples of horizontal gene transfer from animal to prokaryote is the fibronectin type III domain (FnIIID). Certain extracellular proteins of soil bacteria contain an unusual cluster of FnIIIDs, which show sequence similarity to those of animals and are likely to have been acquired horizontally from animals. Here we report the solution structure of the FnIIID of chitinase A1 from Bacillus circulans WL-12. To the best of our knowledge, this is the first tertiary structure to be reported for an FnIIID from a bacterial protein. The structure of the domain shows significant similarity to FnIIIDs from animal proteins. Sequence comparisons with FnIIIDs from other soil bacteria proteins show that the core-forming residues are highly conserved and, thus, are under strong evolutionary pressure. Striking similarities in the tertiary structures of bacterial FnIIIDs and their mammalian counterparts may support the hypothesis that the evolution of the FnIIID in bacterial carbohydrases occurred horizontally. The total lack of surface-exposed aromatic residues also suggests that the role of this FnIIID is different from those of other bacterial beta-sandwich domains, which function as carbohydrate-binding modules.

PubMed: 11600504
DOI: 10.1074/jbc.M109726200

Experimental method

SOLUTION NMR