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New page: left|200px<br /><applet load="2blg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2blg, resolution 2.46Å" /> '''STRUCTURAL BASIS OF ...
 
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[[Image:2blg.gif|left|200px]]<br /><applet load="2blg" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2blg, resolution 2.46&Aring;" />
'''STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 8.2'''<br />


==Overview==
==STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 8.2==
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.
<StructureSection load='2blg' size='340' side='right'caption='[[2blg]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2blg]] 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=2BLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BLG 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]] 2.46&#8491;</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=2blg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2blg OCA], [https://pdbe.org/2blg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2blg RCSB], [https://www.ebi.ac.uk/pdbsum/2blg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2blg ProSAT]</span></td></tr>
</table>
== Function ==
[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.
== 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/bl/2blg_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=2blg ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==About this Structure==
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>
2BLG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BLG OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9760236 9760236]
</div>
<div class="pdbe-citations 2blg" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Baker, E.N.]]
[[Category: Baker EN]]
[[Category: Baker, H.M.]]
[[Category: Baker HM]]
[[Category: Bewley, M.C.]]
[[Category: Bewley MC]]
[[Category: Creamer, L.K.]]
[[Category: Creamer LK]]
[[Category: Jameson, G.B.]]
[[Category: Jameson GB]]
[[Category: Qin, B.Y.]]
[[Category: Qin BY]]
[[Category: beta-lactoglobulin]]
[[Category: crystal structure]]
[[Category: loop movement]]
[[Category: ph-dependent conformation]]
[[Category: tanford transition]]
[[Category: transport]]
 
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Retrieved from "https://proteopedia.org/2blg"