1t3c: Difference between revisions
New page: left|200px<br /> <applet load="1t3c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t3c, resolution 1.90Å" /> '''Clostridium botulin... |
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==About this Structure== | ==About this Structure== | ||
1T3C 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/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.69 3.4.24.69]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T3C OCA]]. | 1T3C 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]]. Structure known Active Sites: AC1 and AC2. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T3C OCA]]. | ||
==Reference== | ==Reference== | ||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15157097 15157097] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15157097 15157097] | ||
[[Category: Bontoxilysin]] | |||
[[Category: Clostridium botulinum]] | [[Category: Clostridium botulinum]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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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 Oct 30 12:41:50 2007'' | ||
Revision as of 13:37, 30 October 2007
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Clostridium botulinum type E catalytic domain E212Q mutant
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 ... [(full description)]
About this StructureAbout this Structure
1T3C 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]. Structure known Active Sites: AC1 and AC2. 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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