1bsy

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[[Image:1bsy.gif|left|200px]]
 
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{{Structure
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==STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 7.1==
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|PDB= 1bsy |SIZE=350|CAPTION= <scene name='initialview01'>1bsy</scene>, resolution 2.24&Aring;
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<StructureSection load='1bsy' size='340' side='right'caption='[[1bsy]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1bsy]] 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=1BSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BSY 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]] 2.24&#8491;</td></tr>
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|GENE=
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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=1bsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bsy OCA], [https://pdbe.org/1bsy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bsy RCSB], [https://www.ebi.ac.uk/pdbsum/1bsy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bsy ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1bsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bsy OCA], [http://www.ebi.ac.uk/pdbsum/1bsy PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1bsy RCSB]</span>
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[https://www.uniprot.org/uniprot/LACB_BOVIN LACB_BOVIN] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
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}}
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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/bs/1bsy_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=1bsy 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 structures of the trigonal crystal form of bovine beta-lactoglobulin variant A at pH 6.2, 7.1, and 8.2 have been determined by X-ray diffraction methods at a resolution of 2.56, 2. 24, and 2.49 A, respectively. The corresponding values for R (Rfree) are 0.192 (0.240), 0.234 (0.279), and 0.232 (0.277). The C and N termini as well as two disulfide bonds are clearly defined in these models. The glutamate side chain of residue 89 is buried at pH 6.2 and becomes exposed at pH 7.1 and 8.2. This conformational change, involving the loop 85-90, provides a structural basis for a variety of pH-dependent chemical, physical, and spectroscopic phenomena, collectively known as the Tanford transition.
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'''STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 7.1'''
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Structural basis of the Tanford transition of bovine beta-lactoglobulin.,Qin BY, Bewley MC, Creamer LK, Baker HM, Baker EN, Jameson GB Biochemistry. 1998 Oct 6;37(40):14014-23. PMID:9760236<ref>PMID:9760236</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 1bsy" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The structures of the trigonal crystal form of bovine beta-lactoglobulin variant A at pH 6.2, 7.1, and 8.2 have been determined by X-ray diffraction methods at a resolution of 2.56, 2. 24, and 2.49 A, respectively. The corresponding values for R (Rfree) are 0.192 (0.240), 0.234 (0.279), and 0.232 (0.277). The C and N termini as well as two disulfide bonds are clearly defined in these models. The glutamate side chain of residue 89 is buried at pH 6.2 and becomes exposed at pH 7.1 and 8.2. This conformational change, involving the loop 85-90, provides a structural basis for a variety of pH-dependent chemical, physical, and spectroscopic phenomena, collectively known as the Tanford transition.
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*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1BSY 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=1BSY OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Structural basis of the Tanford transition of bovine beta-lactoglobulin., Qin BY, Bewley MC, Creamer LK, Baker HM, Baker EN, Jameson GB, Biochemistry. 1998 Oct 6;37(40):14014-23. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9760236 9760236]
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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: Baker, E N.]]
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[[Category: Baker EN]]
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[[Category: Bewley, M C.]]
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[[Category: Bewley MC]]
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[[Category: Creamer, L K.]]
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[[Category: Creamer LK]]
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[[Category: Jameson, G B.]]
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[[Category: Jameson GB]]
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[[Category: Qin, B Y.]]
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[[Category: Qin BY]]
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[[Category: beta-lactoglobulin]]
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[[Category: crystal structure]]
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[[Category: loop movement]]
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[[Category: ph-dependent conformation]]
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[[Category: tanford transition]]
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[[Category: transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:07:46 2008''
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Current revision

STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 7.1

PDB ID 1bsy

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