This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1jza

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jza.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1jza.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jza| PDB=1jza | SCENE= }}
{{STRUCTURE_1jza| PDB=1jza | SCENE= }}
-
'''Crystal Structure of Variant 2 Scorpion Toxin from Centruroides sculpturatus Ewing'''
+
===Crystal Structure of Variant 2 Scorpion Toxin from Centruroides sculpturatus Ewing===
-
==Overview==
+
<!--
-
Centruroides sculpturatus Ewing variant 2 toxin (CsE-v2) is a neurotoxin isolated from the venom of a scorpion native to the Arizona desert. The structure of CsE-v2 was solved in two different crystal forms using a combination of molecular replacement and multiple isomorphous replacement techniques. Crystals of CsE-v2 display a temperature-dependent, reversible-phase transition near room temperature. At lower temperature the space group changes from P3(2)21 to P3(1)21 with an approximate doubling of the C-axis. The small-cell structure, which has one molecule per asymmetric unit, has an R factor of 0.229 at 2.8 A resolution. The large-cell structure has two molecules per asymmetric unit and was refined at 2.2 A resolution to an R factor of 0.255. CsE-v2 is a rigid, compact structure with four intrachain disulfide bonds. The structure is similar to other long-chain beta neurotoxins, and the largest differences occur in the last six residues. The high-resolution structure of CsE-v2 corrects an error in the reported C-terminal sequence; the terminal tripeptide sequence is Ser 64-Cys 65-Ser 66 rather than Ser 64-Ser 65-Cys 66. Comparison of CsE-v2 with long-chain alpha toxins reveals four insertions and one deletion, as well as additional residues at the N and C termini. Structural alignment of alpha and beta toxins suggests that the primary distinguishing feature between the two classes is the length of the loop between the second and third strands in a three-strand beta sheet. The shorter loop in alpha toxins exposes a critical lysine side chain, whereas the longer loop in beta toxins buries the corresponding basic residue (either arginine or lysine).
+
The line below this paragraph, {{ABSTRACT_PUBMED_11847271}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11847271 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11847271}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Noncrystallographic symmetry]]
[[Category: Noncrystallographic symmetry]]
[[Category: Scorpion toxin]]
[[Category: Scorpion toxin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:06:21 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 23:53:24 2008''

Revision as of 20:53, 28 July 2008

Template:STRUCTURE 1jza

Crystal Structure of Variant 2 Scorpion Toxin from Centruroides sculpturatus Ewing

Template:ABSTRACT PUBMED 11847271

About this Structure

1JZA is a Single protein structure of sequence from Centruroides sculpturatus. Full crystallographic information is available from OCA.

Reference

Structure of variant 2 scorpion toxin from Centruroides sculpturatus Ewing., Cook WJ, Zell A, Watt DD, Ealick SE, Protein Sci. 2002 Mar;11(3):479-86. PMID:11847271

Page seeded by OCA on Mon Jul 28 23:53:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools