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 2.30&Aring;" /> '''2.3 Angstrom crystal...)
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[[Image:1z7h.gif|left|200px]]<br /><applet load="1z7h" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1z7h.gif|left|200px]]<br /><applet load="1z7h" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1z7h, resolution 2.30&Aring;" />
caption="1z7h, resolution 2.30&Aring;" />
'''2.3 Angstrom crystal structure of tetanus neurotoxin light chain'''<br />
'''2.3 Angstrom crystal structure of tetanus neurotoxin light chain'''<br />
==Overview==
==Overview==
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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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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==
==About this Structure==
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1Z7H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_tetani Clostridium tetani] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tentoxilysin Tentoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.68 3.4.24.68] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z7H OCA].
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1Z7H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_tetani Clostridium tetani] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tentoxilysin Tentoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.68 3.4.24.68] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z7H OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Tentoxilysin]]
[[Category: Tentoxilysin]]
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[[Category: Breidenbach, M.A.]]
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[[Category: Breidenbach, M A.]]
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[[Category: Brunger, A.T.]]
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[[Category: Brunger, A T.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: metalloprotease]]
[[Category: metalloprotease]]
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[[Category: tetanus]]
[[Category: tetanus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:16:54 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:48 2008''

Revision as of 14:12, 21 February 2008


1z7h, resolution 2.30Å

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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 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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