1e1h
From Proteopedia
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| - | [[Image:1e1h.gif|left|200px]]<br /> | + | [[Image:1e1h.gif|left|200px]]<br /><applet load="1e1h" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1e1h" size=" | + | |
caption="1e1h, resolution 1.80Å" /> | caption="1e1h, resolution 1.80Å" /> | ||
'''CRYSTAL STRUCTURE OF RECOMBINANT BOTULINUM NEUROTOXIN TYPE A LIGHT CHAIN, SELF-INHIBITING ZN ENDOPEPTIDASE.'''<br /> | '''CRYSTAL STRUCTURE OF RECOMBINANT BOTULINUM NEUROTOXIN TYPE A LIGHT CHAIN, SELF-INHIBITING ZN ENDOPEPTIDASE.'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E1H is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] | + | 1E1H is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Bontoxilysin Bontoxilysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69] Known structural/functional Site: <scene name='pdbsite=1:Monomer+B+Zn+Endopeptidase+Active+Site.+Zn+(II)+Coordina+...'>1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E1H OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zn-endopeptidase]] | [[Category: zn-endopeptidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 09:36:34 2008'' |
Revision as of 07:36, 3 February 2008
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CRYSTAL STRUCTURE OF RECOMBINANT BOTULINUM NEUROTOXIN TYPE A LIGHT CHAIN, SELF-INHIBITING ZN ENDOPEPTIDASE.
Overview
Clostridium botulinum neurotoxins (BoNTs), the most potent toxins known, disrupt neurotransmission through proteolysis of proteins involved in, neuroexocytosis. The light chains of BoNTs are unique zinc proteases that, have stringent substrate specificity and require exceptionally long, substrates. We have determined the crystal structure of the protease, domain from BoNT serotype A (BoNT/A). The structure reveals a homodimer in, a product-bound state, with loop F242-V257 from each monomer deeply buried, in its partner's catalytic site. The loop, which acts as a substrate, is, oriented in reverse of the canonical direction for other zinc proteases., The Y249-Y250 peptide bond of the substrate loop is hydrolyzed, leaving, the Y249 product carboxylate coordinated to the catalytic zinc. From the, crystal structure of the BoNT/A protease, detailed models of noncanonical, binding and proteolysis can be derived which we propose are also, consistent with BoNT/A binding and proteolysis of natural substrate, synaptosome-associated protein of 25 kDa (SNAP-25). The proposed BoNT/A, substrate-binding mode and catalytic mechanism are markedly different from, those previously proposed for the BoNT serotype B.
About this Structure
1E1H is a Protein complex structure of sequences from Clostridium botulinum with as ligand. Active as Bontoxilysin, with EC number 3.4.24.69 Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
Crystal structure of Clostridium botulinum neurotoxin protease in a product-bound state: Evidence for noncanonical zinc protease activity., Segelke B, Knapp M, Kadkhodayan S, Balhorn R, Rupp B, Proc Natl Acad Sci U S A. 2004 May 4;101(18):6888-93. Epub 2004 Apr 23. PMID:15107500
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