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New page: left|200px<br /><applet load="1kx9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kx9, resolution 1.65Å" /> '''ANTENNAL CHEMOSENSOR... |
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== | ==ANTENNAL CHEMOSENSORY PROTEIN A6 FROM THE MOTH MAMESTRA BRASSICAE== | ||
Chemosensory proteins (CSPs) are believed to be involved in chemical | <StructureSection load='1kx9' size='340' side='right'caption='[[1kx9]], [[Resolution|resolution]] 1.65Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1kx9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mamestra_brassicae Mamestra brassicae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KX9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1kx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kx9 OCA], [https://pdbe.org/1kx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kx9 RCSB], [https://www.ebi.ac.uk/pdbsum/1kx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kx9 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q9NG96_MAMBR Q9NG96_MAMBR] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kx/1kx9_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1kx9 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:12068017</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1kx9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Mamestra brassicae]] | [[Category: Mamestra brassicae]] | ||
[[Category: Cambillau C]] | |||
[[Category: Cambillau | [[Category: Campanacci V]] | ||
[[Category: Campanacci | [[Category: Jones TA]] | ||
[[Category: Jones | [[Category: Larsson AM]] | ||
[[Category: Larsson | [[Category: Lartigue A]] | ||
[[Category: Lartigue | [[Category: Roussel A]] | ||
[[Category: Roussel | [[Category: Tegoni M]] | ||
[[Category: Tegoni | |||
Latest revision as of 09:55, 30 October 2024
ANTENNAL CHEMOSENSORY PROTEIN A6 FROM THE MOTH MAMESTRA BRASSICAEANTENNAL CHEMOSENSORY PROTEIN A6 FROM THE MOTH MAMESTRA BRASSICAE
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedChemosensory 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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