1Z7H

2.3A Crystal structure of tetanus neurotoxin light chain

(2005) Biochemistry 44: 7450-7457

• PubMed: 15895988 Search on PubMed
• DOI: https://doi.org/10.1021/bi050262j
• Primary Citation of Related Structures:  
  1Z7H


• PubMed Abstract: 
  

  TeNT is the causative agent of the neuroparalytic disease tetanus. A key component of TeNT is its light chain, a Zn(2+) endopeptidase that targets SNAREs. Recent structural studies of closely related BoNT endopeptidases indicate that substrate-binding exosites remote from a conserved active site are the primary determinants of substrate specificity. Here we report the 2.3 A X-ray crystal structure of TeNT-LC, determined by combined molecular replacement and MAD phasing. As expected, the overall structure of TeNT-LC is similar to the other known CNT light chain structures, including a conserved thermolysin-like core inserted between structurally distinct amino- and carboxy-terminal regions. Differences between TeNT-LC and the other CNT light chains are mainly limited to surface features such as unique electrostatic potential profiles. An analysis of surface residue conservation reveals a pattern of relatively high variability matching the path of substrate binding around BoNT/A, possibly serving to accommodate the variations in different SNARE targets of the CNT group.

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Organizational Affiliation: 

Department of Molecular and Cellular Physiology, Stanford University, Stanford, California 94305, USA.