1k19

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(New page: 200px<br /><applet load="1k19" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k19" /> '''NMR Solution Structure of the Chemosensory P...)
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'''NMR Solution Structure of the Chemosensory Protein CSP2 from Moth Mamestra brassicae'''<br />
'''NMR Solution Structure of the Chemosensory Protein CSP2 from Moth Mamestra brassicae'''<br />
==Overview==
==Overview==
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Chemosensory proteins (CSPs) are believed to be involved in chemical, communication and perception. A number of such proteins, of molecular mass, approximately 13 kDa, have been isolated from different sensory organs of, a wide range of insect species. Several CSPs have been identified in the, antennae and proboscis of the moth Mamestra brassicae. CSPMbraA6, a, 112-amino-acid antennal protein, has been expressed in a soluble form in, large quantities in the Escherichi coli periplasm. NMR structure, determination of CSPMbraA6 has been performed with 1H- and 15N-labelled, samples. The calculated structures present an average root mean square, deviation about the mean structure of 0.63 A for backbone atoms and 1.27 A, for all non-hydrogen atoms except the 12 N-terminal residues. The protein, is well folded from residue 12 to residue 110, and consists of a, non-bundle alpha-helical structure with six helices connected by alpha, alpha loops. It has a globular shape, with overall dimensions of 32 A x 28, A x 24 A. A channel is visible in the hydrophobic core, with dimensions of, 3 A x 9 A x 21 A. In some of the 20 solution structures calculated, this, channel is closed either by Trp-94 at one end or by Tyr-26 at the other, end; in some other solutions, this channel is closed at both ends. Binding, experiments with 12-bromododecanol indicate that the CSPMbraA6 structure, is modified upon ligand binding.
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Chemosensory proteins (CSPs) are believed to be involved in chemical communication and perception. A number of such proteins, of molecular mass approximately 13 kDa, have been isolated from different sensory organs of a wide range of insect species. Several CSPs have been identified in the antennae and proboscis of the moth Mamestra brassicae. CSPMbraA6, a 112-amino-acid antennal protein, has been expressed in a soluble form in large quantities in the Escherichi coli periplasm. NMR structure determination of CSPMbraA6 has been performed with 1H- and 15N-labelled samples. The calculated structures present an average root mean square deviation about the mean structure of 0.63 A for backbone atoms and 1.27 A for all non-hydrogen atoms except the 12 N-terminal residues. The protein is well folded from residue 12 to residue 110, and consists of a non-bundle alpha-helical structure with six helices connected by alpha alpha loops. It has a globular shape, with overall dimensions of 32 A x 28 A x 24 A. A channel is visible in the hydrophobic core, with dimensions of 3 A x 9 A x 21 A. In some of the 20 solution structures calculated, this channel is closed either by Trp-94 at one end or by Tyr-26 at the other end; in some other solutions, this channel is closed at both ends. Binding experiments with 12-bromododecanol indicate that the CSPMbraA6 structure is modified upon ligand binding.
==About this Structure==
==About this Structure==
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1K19 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mamestra_brassicae Mamestra brassicae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K19 OCA].
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1K19 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mamestra_brassicae Mamestra brassicae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K19 OCA].
==Reference==
==Reference==
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[[Category: pheromone]]
[[Category: pheromone]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 00:32:45 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:28:58 2008''

Revision as of 11:28, 21 February 2008


1k19

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NMR Solution Structure of the Chemosensory Protein CSP2 from Moth Mamestra brassicae

Overview

Chemosensory proteins (CSPs) are believed to be involved in chemical communication and perception. A number of such proteins, of molecular mass approximately 13 kDa, have been isolated from different sensory organs of a wide range of insect species. Several CSPs have been identified in the antennae and proboscis of the moth Mamestra brassicae. CSPMbraA6, a 112-amino-acid antennal protein, has been expressed in a soluble form in large quantities in the Escherichi coli periplasm. NMR structure determination of CSPMbraA6 has been performed with 1H- and 15N-labelled samples. The calculated structures present an average root mean square deviation about the mean structure of 0.63 A for backbone atoms and 1.27 A for all non-hydrogen atoms except the 12 N-terminal residues. The protein is well folded from residue 12 to residue 110, and consists of a non-bundle alpha-helical structure with six helices connected by alpha alpha loops. It has a globular shape, with overall dimensions of 32 A x 28 A x 24 A. A channel is visible in the hydrophobic core, with dimensions of 3 A x 9 A x 21 A. In some of the 20 solution structures calculated, this channel is closed either by Trp-94 at one end or by Tyr-26 at the other end; in some other solutions, this channel is closed at both ends. Binding experiments with 12-bromododecanol indicate that the CSPMbraA6 structure is modified upon ligand binding.

About this Structure

1K19 is a Single protein structure of sequence from Mamestra brassicae. Full crystallographic information is available from OCA.

Reference

Solution structure of a chemosensory protein from the moth Mamestra brassicae., Mosbah A, Campanacci V, Lartigue A, Tegoni M, Cambillau C, Darbon H, Biochem J. 2003 Jan 1;369(Pt 1):39-44. PMID:12217077

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