2hlv

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(New page: 200px {{Structure |PDB= 2hlv |SIZE=350|CAPTION= <scene name='initialview01'>2hlv</scene>, resolution 1.65&Aring; |SITE= <scene name='pdbsite=AC1:Lik+Binding+Site+...)
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[[Image:2hlv.jpg|left|200px]]
 
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{{Structure
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==Bovine Odorant Binding Protein deswapped triple mutant==
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|PDB= 2hlv |SIZE=350|CAPTION= <scene name='initialview01'>2hlv</scene>, resolution 1.65&Aring;
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<StructureSection load='2hlv' size='340' side='right'caption='[[2hlv]], [[Resolution|resolution]] 1.65&Aring;' scene=''>
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|SITE= <scene name='pdbsite=AC1:Lik+Binding+Site+For+Residue+A+999'>AC1</scene> and <scene name='pdbsite=AC2:Gol+Binding+Site+For+Residue+A+201'>AC2</scene>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LIK:3,6-BIS(METHYLENE)DECANOIC+ACID'>LIK</scene>
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<table><tr><td colspan='2'>[[2hlv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HLV FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.65&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=LIK:3,6-BIS(METHYLENE)DECANOIC+ACID'>LIK</scene></td></tr>
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|DOMAIN=<span class='plainlinks'>[http://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=pfam00061 Lipocalin]</span>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2hlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hlv OCA], [https://pdbe.org/2hlv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hlv RCSB], [https://www.ebi.ac.uk/pdbsum/2hlv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hlv ProSAT]</span></td></tr>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hlv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hlv OCA], [http://www.ebi.ac.uk/pdbsum/2hlv PDBsum], [http://www.fli-leibniz.de/cgi-bin/ImgLib.pl?CODE=1kfv JenaLib], [http://www.rcsb.org/pdb/explore.do?structureId=2hlv RCSB]</span>
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</table>
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}}
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== Function ==
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[https://www.uniprot.org/uniprot/OBP_BOVIN OBP_BOVIN] This protein binds a wide variety of chemical odorants.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hl/2hlv_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2hlv ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The X-ray structure of bovine Odorant Binding Protein (bOBP) revealed its association as a domain swapped dimer. bOBP, devoid of any cysteines, contrasts with other mammalian OBPs, which are monomeric and possess at least one disulfide bridge. We have produced a mutant of bOBP in which a glycine residue was inserted after position 121. This mutation yielded a monomeric bOBP-121Gly+ in which domain swapping has been reverted. Here, we have subsequently introduced two mutations, Trp64Cys and His155Cys, in view to stabilize the putative monomer with a disulfide bridge. We have determined the crystal structure of this triple mutant at 1.65 A resolution. The mutant protein is monomeric, stabilized by a disulfide bridge between Trp64Cys and His155Cys, with a backbone superimposable to that of native bOBP, with the exception of the hinge and of the 10 residues at the C-terminus. bOBP triple mutant binds 1-amino-anthracene, 1-octen-3-ol (bOBP co-purified ligand) and other ligands with microM Kd values comparable to those of the swapped dimer.
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'''Bovine Odorant Binding Protein deswapped triple mutant'''
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Deswapping bovine odorant binding protein.,Ramoni R, Spinelli S, Grolli S, Conti V, Merli E, Cambillau C, Tegoni M Biochim Biophys Acta. 2008 Apr;1784(4):651-7. Epub 2008 Jan 29. PMID:18269920<ref>PMID:18269920</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2hlv" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The X-ray structure of bovine Odorant Binding Protein (bOBP) revealed its association as a domain swapped dimer. bOBP, devoid of any cysteines, contrasts with other mammalian OBPs, which are monomeric and possess at least one disulfide bridge. We have produced a mutant of bOBP in which a glycine residue was inserted after position 121. This mutation yielded a monomeric bOBP-121Gly+ in which domain swapping has been reverted. Here, we have subsequently introduced two mutations, Trp64Cys and His155Cys, in view to stabilize the putative monomer with a disulfide bridge. We have determined the crystal structure of this triple mutant at 1.65 A resolution. The mutant protein is monomeric, stabilized by a disulfide bridge between Trp64Cys and His155Cys, with a backbone superimposable to that of native bOBP, with the exception of the hinge and of the 10 residues at the C-terminus. bOBP triple mutant binds 1-amino-anthracene, 1-octen-3-ol (bOBP co-purified ligand) and other ligands with muM Kd values comparable to those of the swapped dimer.
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*[[Odorant binding protein 3D structures|Odorant binding protein 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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2HLV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HLV OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Deswapping bovine odorant binding protein., Ramoni R, Spinelli S, Grolli S, Conti V, Merli E, Cambillau C, Tegoni M, Biochim Biophys Acta. 2008 Apr;1784(4):651-7. Epub 2008 Jan 29. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18269920 18269920]
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cambillau, C.]]
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[[Category: Cambillau C]]
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[[Category: Spinelli, S.]]
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[[Category: Spinelli S]]
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[[Category: Tegoni, M.]]
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[[Category: Tegoni M]]
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[[Category: domain swapping]]
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[[Category: odorant binding protein]]
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[[Category: transport protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Mar 26 09:51:16 2008''
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Current revision

Bovine Odorant Binding Protein deswapped triple mutant

PDB ID 2hlv

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