1jzb: Difference between revisions

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[[Image:1jzb.gif|left|200px]]<br /><applet load="1jzb" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1jzb.gif|left|200px]]<br /><applet load="1jzb" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1jzb, resolution 2.81Å" />

'''Crystal Structure of Variant 2 Scorpion Toxin from Centruroides sculpturatus Ewing'''<br />

==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).

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).

==About this Structure==

1JZB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Centruroides_sculpturatus Centruroides sculpturatus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1JZB OCA].

1JZB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Centruroides_sculpturatus Centruroides sculpturatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZB OCA].

==Reference==

Line 13:

[[Category: Centruroides sculpturatus]]

[[Category: Single protein]]

[[Category: Cook, W.J.]]

[[Category: Cook, W J.]]

[[Category: Ealick, S.E.]]

[[Category: Ealick, S E.]]

[[Category: Watt, D.D.]]

[[Category: Watt, D D.]]

[[Category: Zell, A.]]

[[Category: crystal structure]]

Line 21:

[[Category: scorpion toxin]]

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@@ Line 1: / Line 1: @@
-[[Image:1jzb.gif|left|200px]]<br /><applet load="1jzb" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1jzb.gif|left|200px]]<br /><applet load="1jzb" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1jzb, resolution 2.81&Aring;" />
 '''Crystal Structure of Variant 2 Scorpion Toxin from Centruroides sculpturatus Ewing'''<br />
 ==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).
+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).
 ==About this Structure==
-JZB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Centruroides_sculpturatus Centruroides sculpturatus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JZB OCA].
+JZB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Centruroides_sculpturatus Centruroides sculpturatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JZB OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Centruroides sculpturatus]]
 [[Category: Single protein]]
-[[Category: Cook, W.J.]]
+[[Category: Cook, W J.]]
-[[Category: Ealick, S.E.]]
+[[Category: Ealick, S E.]]
-[[Category: Watt, D.D.]]
+[[Category: Watt, D D.]]
 [[Category: Zell, A.]]
 [[Category: crystal structure]]
@@ Line 21: / Line 21: @@
 [[Category: scorpion toxin]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:42:56 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:24 2008''