1kx9: Difference between revisions

Revision as of 14:38, 21 February 2008

ANTENNAL CHEMOSENSORY PROTEIN A6 FROM THE MOTH MAMESTRA BRASSICAE

OverviewOverview

Chemosensory proteins (CSPs) are believed to be involved in chemical communication and perception. Such proteins, of M(r) 13,000, have been isolated from several sensory organs of a wide range of insect species. Several CSPs have been identified in the antennae and proboscis of the moth Mamestra brassicae. One of them, CSPMbraA6, a 112-amino acid antennal protein, has been expressed in large quantities and is soluble in the Escherichia coli periplasm. X-ray structure determination has been performed in parallel with ligand binding assays using tryptophan fluorescence quenching. The protein has overall dimensions of 25 x 30 x 32 A and exhibits a novel type of alpha-helical fold with six helices connected by alpha-alpha loops. A narrow channel extends within the protein hydrophobic core. Fluorescence quenching with brominated alkyl alcohols or fatty acids and modeling studies indicates that CSPMbraA6 is able to bind such compounds with C12-18 alkyl chains. These ubiquitous proteins might have the role of extracting hydrophobic linear compounds (pheromones, odors, or fatty acids) dispersed in the phospholipid membrane and transporting them to their receptor.

About this StructureAbout this Structure

1KX9 is a Single protein structure of sequence from Mamestra brassicae with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

X-ray structure and ligand binding study of a moth chemosensory protein., Lartigue A, Campanacci V, Roussel A, Larsson AM, Jones TA, Tegoni M, Cambillau C, J Biol Chem. 2002 Aug 30;277(35):32094-8. Epub 2002 Jun 14. PMID:12068017

Page seeded by OCA on Thu Feb 21 13:38:56 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1kx9.gif|left|200px]]<br /><applet load="1kx9" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1kx9.gif|left|200px]]<br /><applet load="1kx9" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1kx9, resolution 1.65&Aring;" />
 '''ANTENNAL CHEMOSENSORY PROTEIN A6 FROM THE MOTH MAMESTRA BRASSICAE'''<br />
 ==Overview==
-Chemosensory proteins (CSPs) are believed to be involved in chemical, communication and perception. Such proteins, of M(r) 13,000, have been, isolated from several sensory organs of a wide range of insect species., Several CSPs have been identified in the antennae and proboscis of the, moth Mamestra brassicae. One of them, CSPMbraA6, a 112-amino acid antennal, protein, has been expressed in large quantities and is soluble in the, Escherichia coli periplasm. X-ray structure determination has been, performed in parallel with ligand binding assays using tryptophan, fluorescence quenching. The protein has overall dimensions of 25 x 30 x 32, A and exhibits a novel type of alpha-helical fold with six helices, connected by alpha-alpha loops. A narrow channel extends within the, protein hydrophobic core. Fluorescence quenching with brominated alkyl, alcohols or fatty acids and modeling studies indicates that CSPMbraA6 is, able to bind such compounds with C12-18 alkyl chains. These ubiquitous, proteins might have the role of extracting hydrophobic linear compounds, (pheromones, odors, or fatty acids) dispersed in the phospholipid membrane, and transporting them to their receptor.
+Chemosensory proteins (CSPs) are believed to be involved in chemical communication and perception. Such proteins, of M(r) 13,000, have been isolated from several sensory organs of a wide range of insect species. Several CSPs have been identified in the antennae and proboscis of the moth Mamestra brassicae. One of them, CSPMbraA6, a 112-amino acid antennal protein, has been expressed in large quantities and is soluble in the Escherichia coli periplasm. X-ray structure determination has been performed in parallel with ligand binding assays using tryptophan fluorescence quenching. The protein has overall dimensions of 25 x 30 x 32 A and exhibits a novel type of alpha-helical fold with six helices connected by alpha-alpha loops. A narrow channel extends within the protein hydrophobic core. Fluorescence quenching with brominated alkyl alcohols or fatty acids and modeling studies indicates that CSPMbraA6 is able to bind such compounds with C12-18 alkyl chains. These ubiquitous proteins might have the role of extracting hydrophobic linear compounds (pheromones, odors, or fatty acids) dispersed in the phospholipid membrane and transporting them to their receptor.
 ==About this Structure==
-KX9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mamestra_brassicae Mamestra brassicae] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KX9 OCA].
+KX9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mamestra_brassicae Mamestra brassicae] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KX9 OCA].
 ==Reference==
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 [[Category: Cambillau, C.]]
 [[Category: Campanacci, V.]]
-[[Category: Jones, T.A.]]
+[[Category: Jones, T A.]]
-[[Category: Larsson, A.M.]]
+[[Category: Larsson, A M.]]
 [[Category: Lartigue, A.]]
 [[Category: Roussel, A.]]
@@ Line 23: / Line 23: @@
 [[Category: all helix]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 02:07:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:38:56 2008''