A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation

Jeffrey J. Wilson, Osamu Matsushita, Akinobu Okabe, Joshua Sakon

Research output: Contribution to journalArticlepeer-review

96 Citations (Scopus)


The crystal structure of a collagen-binding domain (CBD) with an N-terminal domain linker from Clostridium histolyticum class I collagenase was determined at 1.00 Å resolution in the absence of calcium (1NQJ) and at 1.65 Å resolution in the presence of calcium (1NQD). The mature enzyme is composed of four domains: a metalloprotease domain, a spacing domain and two CBDs. A 12-residue-long linker is found at the N-terminus of each CBD. In the absence of calcium, the CBD reveals a β-sheet sandwich fold with the linker adopting an α-helix. The addition of calcium unwinds the linker and anchors it to the distal side of the sandwich as a new β-strand. The conformational change of the linker upon calcium binding is confirmed by changes in the Stokes and hydrodynamic radii as measured by size exclusion chromatography and by dynamic light scattering with and without calcium. Furthermore, extensive mutagenesis of conserved surface residues and collagen-binding studies allow us to identify the collagen-binding surface of the protein and propose likely collagen-protein binding models.

Original languageEnglish
Pages (from-to)1743-1752
Number of pages10
JournalEMBO Journal
Issue number8
Publication statusPublished - Apr 15 2003
Externally publishedYes


  • Calcium-induced conformational change
  • Domain reorientation
  • Extracellular calcium-binding protein
  • Molecular switch
  • Square antiprismatic

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)


Dive into the research topics of 'A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation'. Together they form a unique fingerprint.

Cite this