1qwv: Difference between revisions

← Older edit

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1qwv.gif|left|200px]]
- {{Structure
+==Solution structure of Antheraea polyphemus pheromone binding protein (ApolPBP)==
-|PDB= 1qwv |SIZE=350|CAPTION= <scene name='initialview01'>1qwv</scene>
+<StructureSection load='1qwv' size='340' side='right'caption='[[1qwv]]' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[1qwv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Antheraea_polyphemus Antheraea polyphemus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QWV FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
-|GENE=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwv OCA], [https://pdbe.org/1qwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qwv RCSB], [https://www.ebi.ac.uk/pdbsum/1qwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qwv ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=[[1ls8|1LS8]]
+== Function ==
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qwv OCA], [http://www.ebi.ac.uk/pdbsum/1qwv PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qwv RCSB]</span>
+[https://www.uniprot.org/uniprot/PBP_ANTPO PBP_ANTPO] This major soluble protein in olfactory sensilla of male moths might serve to solubilize the extremely hydrophobic pheromone molecules and to transport pheromone through the aqueous lymph to receptors located on olfactory cilia.
-}}
+== 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/qw/1qwv_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=1qwv ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Pheromone-binding proteins (PBPs) located in the antennae of male moth species play an important role in olfaction. They are carrier proteins, believed to transport volatile hydrophobic pheromone molecules across the aqueous sensillar lymph to the membrane-bound G protein-coupled olfactory receptor proteins. The roles of PBPs in molecular recognition and the mechanisms of pheromone binding and release are poorly understood. Here, we report the NMR structure of a PBP from the giant silk moth Antheraea polyphemus. This is the first structure of a PBP with specific acetate-binding function in vivo. The protein consists of nine alpha-helices: alpha1a (residues 2-5), alpha1b (8-12), alpha1c (16-23), alpha2 (27-34), alpha3a (46-52), alpha3b (54-59), alpha4 (70-79), alpha5 (84-100) and alpha6 (107-125), held together by three disulfide bridges: 19-54, 50-108 and 97-117. A large hydrophobic cavity is located inside the protein, lined with side-chains from all nine helices. The acetate-binding site is located at the narrow end of the cavity formed by the helices alpha3b and alpha4. The pheromone can enter this cavity through an opening between the helix alpha1a, the C-terminal end of the helix alpha6, and the loop between alpha2 and alpha3a. We suggest that Trp37 may play an important role in the initial interaction with the ligand. Our analysis also shows that Asn53 plays the key role in recognition of acetate pheromones specifically, while Phe12, Phe36, Trp37, Phe76, and Phe118 are responsible for non-specific binding, and Leu8 and Ser9 may play a role in ligand chain length recognition.
-'''Solution structure of Antheraea polyphemus pheromone binding protein (ApolPBP)'''
+The solution NMR structure of Antheraea polyphemus PBP provides new insight into pheromone recognition by pheromone-binding proteins.,Mohanty S, Zubkov S, Gronenborn AM J Mol Biol. 2004 Mar 19;337(2):443-51. PMID:15003458<ref>PMID:15003458</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1qwv" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-Pheromone-binding proteins (PBPs) located in the antennae of male moth species play an important role in olfaction. They are carrier proteins, believed to transport volatile hydrophobic pheromone molecules across the aqueous sensillar lymph to the membrane-bound G protein-coupled olfactory receptor proteins. The roles of PBPs in molecular recognition and the mechanisms of pheromone binding and release are poorly understood. Here, we report the NMR structure of a PBP from the giant silk moth Antheraea polyphemus. This is the first structure of a PBP with specific acetate-binding function in vivo. The protein consists of nine alpha-helices: alpha1a (residues 2-5), alpha1b (8-12), alpha1c (16-23), alpha2 (27-34), alpha3a (46-52), alpha3b (54-59), alpha4 (70-79), alpha5 (84-100) and alpha6 (107-125), held together by three disulfide bridges: 19-54, 50-108 and 97-117. A large hydrophobic cavity is located inside the protein, lined with side-chains from all nine helices. The acetate-binding site is located at the narrow end of the cavity formed by the helices alpha3b and alpha4. The pheromone can enter this cavity through an opening between the helix alpha1a, the C-terminal end of the helix alpha6, and the loop between alpha2 and alpha3a. We suggest that Trp37 may play an important role in the initial interaction with the ligand. Our analysis also shows that Asn53 plays the key role in recognition of acetate pheromones specifically, while Phe12, Phe36, Trp37, Phe76, and Phe118 are responsible for non-specific binding, and Leu8 and Ser9 may play a role in ligand chain length recognition.
+*[[Pheromone binding protein|Pheromone binding protein]]
+== References ==
-==About this Structure==
+<references/>
-QWV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Antheraea_polyphemus Antheraea polyphemus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QWV OCA].
+__TOC__
+</StructureSection>
-==Reference==
-The solution NMR structure of Antheraea polyphemus PBP provides new insight into pheromone recognition by pheromone-binding proteins., Mohanty S, Zubkov S, Gronenborn AM, J Mol Biol. 2004 Mar 19;337(2):443-51. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15003458 15003458]
 [[Category: Antheraea polyphemus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Gronenborn, A M.]]
+[[Category: Gronenborn AM]]
-[[Category: Mohanty, S.]]
+[[Category: Mohanty S]]
-[[Category: Zubkov, S.]]
+[[Category: Zubkov S]]
-[[Category: antheraea polyphemus]]
-[[Category: apolpbp]]
-[[Category: hexahelical fold]]
-[[Category: pbp]]
-[[Category: pbp fold]]
-[[Category: pheromone binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:20:07 2008''