1t7b

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(New page: 200px<br /><applet load="1t7b" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t7b, resolution 1.85&Aring;" /> '''Crystal structure of...)
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[[Image:1t7b.jpg|left|200px]]<br /><applet load="1t7b" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1t7b, resolution 1.85&Aring;" />
caption="1t7b, resolution 1.85&Aring;" />
'''Crystal structure of mutant Lys8Gln of scorpion alpha-like neurotoxin BmK M1 from Buthus martensii Karsch'''<br />
'''Crystal structure of mutant Lys8Gln of scorpion alpha-like neurotoxin BmK M1 from Buthus martensii Karsch'''<br />
==Overview==
==Overview==
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Non-proline cis peptide bonds have been observed in numerous protein, crystal structures even though the energetic barrier to this conformation, is significant and no non-prolyl-cis/trans-isomerase has been identified, to date. While some external factors, such as metal binding or co-factor, interaction, have been identified that appear to induce cis/trans, isomerization of non-proline peptide bonds, the intrinsic structural basis, for their existence and the mechanism governing cis/trans isomerization in, proteins remains poorly understood. Here, we report the crystal structure, of a newly isolated neurotoxin, the scorpion alpha-like toxin Buthus, martensii Karsch (BmK) M7, at 1.4A resolution. BmK M7 crystallizes as a, dimer in which the identical non-proline peptide bond between residues 9, and 10 exists either in the cis conformation or as a mixture of cis and, trans conformations in either monomer. We also determined the crystal, structures of several mutants of BmK M1, a representative scorpion, alpha-like toxin that contains an identical non-proline cis peptide bond, as that observed in BmK M7, in which residues within or neighboring the, cis peptide bond were altered. Substitution of an aspartic acid residue, for lysine at residue 8 in the BmK M1 (K8D) mutant converted the cis form, of the non-proline peptide bond 9-10 into the trans form, revealing an, intramolecular switch for cis-to-trans isomerization. Cis/trans, interconversion of the switch residue at position 8 appears to be, sequence-dependent as the peptide bond between residues 9 and 10 retains, its wild-type cis conformation in the BmK M1 (K8Q) mutant structure. The, structural interconversion of the isomeric states of the BmK M1, non-proline cis peptide bond may relate to the conversion of the scorpion, alpha-toxins subgroups.
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Non-proline cis peptide bonds have been observed in numerous protein crystal structures even though the energetic barrier to this conformation is significant and no non-prolyl-cis/trans-isomerase has been identified to date. While some external factors, such as metal binding or co-factor interaction, have been identified that appear to induce cis/trans isomerization of non-proline peptide bonds, the intrinsic structural basis for their existence and the mechanism governing cis/trans isomerization in proteins remains poorly understood. Here, we report the crystal structure of a newly isolated neurotoxin, the scorpion alpha-like toxin Buthus martensii Karsch (BmK) M7, at 1.4A resolution. BmK M7 crystallizes as a dimer in which the identical non-proline peptide bond between residues 9 and 10 exists either in the cis conformation or as a mixture of cis and trans conformations in either monomer. We also determined the crystal structures of several mutants of BmK M1, a representative scorpion alpha-like toxin that contains an identical non-proline cis peptide bond as that observed in BmK M7, in which residues within or neighboring the cis peptide bond were altered. Substitution of an aspartic acid residue for lysine at residue 8 in the BmK M1 (K8D) mutant converted the cis form of the non-proline peptide bond 9-10 into the trans form, revealing an intramolecular switch for cis-to-trans isomerization. Cis/trans interconversion of the switch residue at position 8 appears to be sequence-dependent as the peptide bond between residues 9 and 10 retains its wild-type cis conformation in the BmK M1 (K8Q) mutant structure. The structural interconversion of the isomeric states of the BmK M1 non-proline cis peptide bond may relate to the conversion of the scorpion alpha-toxins subgroups.
==About this Structure==
==About this Structure==
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1T7B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T7B OCA].
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1T7B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mesobuthus_martensii Mesobuthus martensii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T7B OCA].
==Reference==
==Reference==
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[[Category: Mesobuthus martensii]]
[[Category: Mesobuthus martensii]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Guan, R.J.]]
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[[Category: Guan, R J.]]
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[[Category: He, X.L.]]
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[[Category: He, X L.]]
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[[Category: Sundberg, E.J.]]
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[[Category: Sundberg, E J.]]
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[[Category: Wang, C.G.]]
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[[Category: Wang, C G.]]
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[[Category: Wang, D.C.]]
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[[Category: Wang, D C.]]
[[Category: Wang, M.]]
[[Category: Wang, M.]]
[[Category: Xiang, Y.]]
[[Category: Xiang, Y.]]
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[[Category: scorpion toxin]]
[[Category: scorpion toxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 03:02:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:10:38 2008''

Revision as of 13:10, 21 February 2008


1t7b, resolution 1.85Å

Drag the structure with the mouse to rotate

Crystal structure of mutant Lys8Gln of scorpion alpha-like neurotoxin BmK M1 from Buthus martensii Karsch

Overview

Non-proline cis peptide bonds have been observed in numerous protein crystal structures even though the energetic barrier to this conformation is significant and no non-prolyl-cis/trans-isomerase has been identified to date. While some external factors, such as metal binding or co-factor interaction, have been identified that appear to induce cis/trans isomerization of non-proline peptide bonds, the intrinsic structural basis for their existence and the mechanism governing cis/trans isomerization in proteins remains poorly understood. Here, we report the crystal structure of a newly isolated neurotoxin, the scorpion alpha-like toxin Buthus martensii Karsch (BmK) M7, at 1.4A resolution. BmK M7 crystallizes as a dimer in which the identical non-proline peptide bond between residues 9 and 10 exists either in the cis conformation or as a mixture of cis and trans conformations in either monomer. We also determined the crystal structures of several mutants of BmK M1, a representative scorpion alpha-like toxin that contains an identical non-proline cis peptide bond as that observed in BmK M7, in which residues within or neighboring the cis peptide bond were altered. Substitution of an aspartic acid residue for lysine at residue 8 in the BmK M1 (K8D) mutant converted the cis form of the non-proline peptide bond 9-10 into the trans form, revealing an intramolecular switch for cis-to-trans isomerization. Cis/trans interconversion of the switch residue at position 8 appears to be sequence-dependent as the peptide bond between residues 9 and 10 retains its wild-type cis conformation in the BmK M1 (K8Q) mutant structure. The structural interconversion of the isomeric states of the BmK M1 non-proline cis peptide bond may relate to the conversion of the scorpion alpha-toxins subgroups.

About this Structure

1T7B is a Single protein structure of sequence from Mesobuthus martensii. Full crystallographic information is available from OCA.

Reference

Structural mechanism governing cis and trans isomeric states and an intramolecular switch for cis/trans isomerization of a non-proline peptide bond observed in crystal structures of scorpion toxins., Guan RJ, Xiang Y, He XL, Wang CG, Wang M, Zhang Y, Sundberg EJ, Wang DC, J Mol Biol. 2004 Aug 27;341(5):1189-204. PMID:15321715

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