1zn3: Difference between revisions

Revision as of 14:57, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1zn3.png

Template:STRUCTURE 1zn3

Crystal structure of Glu335Ala mutant of Clostridium botulinum neurotoxin type ECrystal structure of Glu335Ala mutant of Clostridium botulinum neurotoxin type E

Template:ABSTRACT PUBMED 15938619

About this StructureAbout this Structure

1ZN3 is a Single protein structure of sequence from Clostridium botulinum. Full crystallographic information is available from OCA.

ReferenceReference

Analysis of active site residues of botulinum neurotoxin E by mutational, functional, and structural studies: Glu335Gln is an apoenzyme., Agarwal R, Binz T, Swaminathan S, Biochemistry. 2005 Jun 14;44(23):8291-302. PMID:15938619

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OCA

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-'''Crystal structure of Glu335Ala mutant of Clostridium botulinum neurotoxin type E'''
+===Crystal structure of Glu335Ala mutant of Clostridium botulinum neurotoxin type E===
-==Overview==
+<!--
-Clostridial neurotoxins comprising the seven serotypes of botulinum neurotoxins and tetanus neurotoxin are the most potent toxins known to humans. Their potency coupled with their specificity and selectivity underscores the importance in understanding their mechanism of action in order to develop a strategy for designing counter measures against them. To develop an effective vaccine against the toxin, it is imperative to achieve an inactive form of the protein which preserves the overall conformation and immunogenicity. Inactive mutants can be achieved either by targeting active site residues or by modifying the surface charges farther away from the active site. The latter affects the long-range forces such as electrostatic potentials in a subtle way without disturbing the structural integrity of the toxin causing some drastic changes in the activity/environment. Here we report structural and biochemical analysis on several mutations on Clostridium botulinum neurotoxin type E light chain with at least two producing dramatic effects: Glu335Gln causes the toxin to transform into a persistent apoenzyme devoid of zinc, and Tyr350Ala has no hydrolytic activity. The structural analysis of several mutants has led to a better understanding of the catalytic mechanism of this family of proteins. The residues forming the S1' subsite have been identified by comparing this structure with a thermolysin-inhibitor complex structure.
+The line below this paragraph, {{ABSTRACT_PUBMED_15938619}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15938619 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15938619}}
 ==About this Structure==
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 [[Category: Glu335ala mutant]]
 [[Category: Light chain]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:49:59 2008''
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