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1bsq

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(New page: 200px<br /><applet load="1bsq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bsq, resolution 2.22&Aring;" /> '''STRUCTURAL AND FUNCT...)
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[[Image:1bsq.gif|left|200px]]<br /><applet load="1bsq" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bsq, resolution 2.22&Aring;" />
 
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'''STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF POINT MUTATIONS OF VARIANTS A AND B OF BOVINE BETA-LACTOGLOBULIN'''<br />
 
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==Overview==
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==STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF POINT MUTATIONS OF VARIANTS A AND B OF BOVINE BETA-LACTOGLOBULIN==
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The structure of the trigonal crystal form of bovine beta-lactoglobulin, variant B at pH 7.1 has been determined by X-ray diffraction methods at a, resolution of 2.22 A and refined to values for R and Rfree of 0.239 and, 0.286, respectively. By comparison with the structure of the trigonal, crystal form of bovine beta-lactoglobulin variant A at pH 7.1, which was, determined previously [Qin BY et al., 1998, Biochemistry 37:14014-14023], the structural consequences of the sequence differences D64G and V118A of, variants A and B, respectively, have been investigated. Only minor, differences in the core calyx structure occur. In the vicinity of the, mutation site D64G on loop CD (residues 61-67), there are small changes in, main-chain conformation, whereas the substitution V118A on beta-strand H, is unaccompanied by changes in the surrounding structure, thereby creating, a void volume and weakened hydrophobic interactions with a consequent loss, of thermal stability relative to variant A. A conformational difference is, found for the loop EF, implicated in the pH-dependent conformational, change known as the Tanford transition, but it is not clear whether this, reflects differences intrinsic to the variants in solution or differences, in crystallization.
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<StructureSection load='1bsq' size='340' side='right'caption='[[1bsq]], [[Resolution|resolution]] 2.22&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bsq]] 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=1BSQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BSQ FirstGlance]. <br>
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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]] 2.22&#8491;</td></tr>
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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=1bsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bsq OCA], [https://pdbe.org/1bsq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bsq RCSB], [https://www.ebi.ac.uk/pdbsum/1bsq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bsq ProSAT]</span></td></tr>
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</table>
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== Function ==
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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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== 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/1bsq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1bsq ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1BSQ 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=1BSQ OCA].
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*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Functional implications of structural differences between variants A and B of bovine beta-lactoglobulin., Qin BY, Bewley MC, Creamer LK, Baker EN, Jameson GB, Protein Sci. 1999 Jan;8(1):75-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10210185 10210185]
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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: bovine beta-lactoglobulin]]
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[[Category: crystal structure]]
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[[Category: genetic variants]]
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[[Category: hydrophobic]]
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[[Category: point mutation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:53:30 2007''
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Current revision

STRUCTURAL AND FUNCTIONAL CONSEQUENCES OF POINT MUTATIONS OF VARIANTS A AND B OF BOVINE BETA-LACTOGLOBULIN

PDB ID 1bsq

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