1t3a: Difference between revisions
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[[Image:1t3a. | [[Image:1t3a.jpg|left|200px]]<br /><applet load="1t3a" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1t3a" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="1t3a, resolution 2.16Å" /> | caption="1t3a, resolution 2.16Å" /> | ||
'''Crystal structure of Clostridium botulinum neurotoxin type E catalytic domain'''<br /> | '''Crystal structure of Clostridium botulinum neurotoxin type E catalytic domain'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1T3A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] with ZN and CL as [http://en.wikipedia.org/wiki/ligands ligands]. 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] | 1T3A is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Clostridium_botulinum Clostridium botulinum] with ZN and CL as [http://en.wikipedia.org/wiki/ligands ligands]. 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 Sites: <scene name='pdbsite=AC1:Zn Binding Site'>AC1</scene> and <scene name='pdbsite=AC2:Zn Binding Site'>AC2</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T3A OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: light chain]] | [[Category: light chain]] | ||
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:01:13 2007'' | ||
Revision as of 18:51, 18 December 2007
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Crystal structure of Clostridium botulinum neurotoxin type E catalytic domain
OverviewOverview
The seven serotypes of botulinum neurotoxins (A-G) produced by Clostridium, botulinum share significant sequence homology and structural similarity., The functions of their individual domains and the modes of action are also, similar. However, the substrate specificity and the peptide bond cleavage, selectivity of their catalytic domains are different. The reason for this, unique specificity of botulinum neurotoxins is still baffling. If an, inhibitor leading to a therapeutic drug common to all serotypes is to be, developed, it is essential to understand the differences in their, three-dimensional structures that empower them with this unique, characteristic. Accordingly, high-resolution structures of all serotypes, are required, and toward achieving this goal the crystal structure of the, catalytic domain of C. botulinum neurotoxin type E has been determined to, 2.1 A resolution. The crystal structure of the inactive mutant, Glu212-->Gln of this protein has also been determined. While the overall, conformation is unaltered in the active site, the position of the, nucleophilic water changes in the mutant, thereby causing it to lose its, ability to activate the catalytic reaction. The structure explains the, importance of the nucleophilic water and the charge on Glu212. The, structural differences responsible for the loss of activity of the mutant, provide a common model for the catalytic pathway of Clostridium, neurotoxins since Glu212 is conserved and has a similar role in all, serotypes. This or a more nonconservative mutant (e.g., Glu212-->Ala), could provide a novel, genetically modified protein vaccine for botulinum.
About this StructureAbout this Structure
1T3A is a Single protein structure of sequence from Clostridium botulinum with ZN and CL as ligands. Active as Bontoxilysin, with EC number 3.4.24.69 Known structural/functional Sites: and . Full crystallographic information is available from OCA.
ReferenceReference
Structural analysis of botulinum neurotoxin type E catalytic domain and its mutant Glu212-->Gln reveals the pivotal role of the Glu212 carboxylate in the catalytic pathway., Agarwal R, Eswaramoorthy S, Kumaran D, Binz T, Swaminathan S, Biochemistry. 2004 Jun 1;43(21):6637-44. PMID:15157097
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