1z7h
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(New page: 200px<br /><applet load="1z7h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z7h, resolution 2.30Å" /> '''2.3 Angstrom crystal...)
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Revision as of 05:09, 21 November 2007
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2.3 Angstrom crystal structure of tetanus neurotoxin light chain
Overview
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.
About this Structure
1Z7H is a Single protein structure of sequence from Clostridium tetani with ZN as ligand. Active as Tentoxilysin, with EC number 3.4.24.68 Full crystallographic information is available from OCA.
Reference
2.3 A crystal structure of tetanus neurotoxin light chain., Breidenbach MA, Brunger AT, Biochemistry. 2005 May 24;44(20):7450-7. PMID:15895988
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