1Z7H

2.3 Angstrom crystal structure of tetanus neurotoxin light chain

Summary for 1Z7H

• Entry DOI: 10.2210/pdb1z7h/pdb
• Descriptor: Tetanus toxin light chain, ZINC ION (3 entities in total)
• Functional Keywords: tent, tetanus, metalloprotease, snare, neurotransmission, hydrolase
• Biological source: Clostridium tetani
• Total number of polymer chains: 1
• Total formula weight: 51352.74

Authors

Breidenbach, M.A.,Brunger, A.T. (deposition date: 2005-03-24, release date: 2005-05-10, Last modification date: 2023-08-23)

Primary citation

Breidenbach, M.A.,Brunger, A.T.
2.3A Crystal structure of tetanus neurotoxin light chain
Biochemistry, 44:7450-7457, 2005

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.

PubMed: 15895988
DOI: 10.1021/bi050262j

Experimental method

X-RAY DIFFRACTION (2.3 Å)