1dv9

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(New page: 200px<br /><applet load="1dv9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dv9" /> '''STRUCTURAL CHANGES ACCOMPANYING PH-INDUCED D...)
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[[Image:1dv9.gif|left|200px]]<br /><applet load="1dv9" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1dv9" />
 
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'''STRUCTURAL CHANGES ACCOMPANYING PH-INDUCED DISSOCIATION OF THE B-LACTOGLOBULIN DIMER'''<br />
 
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==Overview==
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==STRUCTURAL CHANGES ACCOMPANYING PH-INDUCED DISSOCIATION OF THE B-LACTOGLOBULIN DIMER==
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We have used NMR spectroscopy to determine the three-dimensional (3D), structure, and to characterize the backbone dynamics, of a recombinant, version of bovine beta-lactoglobulin (variant A) at pH 2. 6, where the, protein is a monomer. The structure of this low-pH form of, beta-lactoglobulin is very similar to that of a subunit within the dimer, at pH 6.2. The root-mean-square deviation from the pH 6.2 (crystal), structure, calculated for backbone atoms of residues 6-160, is, approximately 1.3 A. Differences arise from the orientation, with respect, to the calyx, of the A-B and C-D loops, and of the flanking three-turn, alpha-helix. The hydrophobic cavity within the calyx is retained at low, pH. The E-F loop (residues 85-90), which moves to occlude the opening of, the cavity over the pH range 7.2-6.2, is in the "closed" position at pH, 2.6, and the side chain of Glu89 is buried. We also carried out, measurements of (15)N T(1)s and T(2)s and (1)H-(15)N heteronuclear NOEs at, pH 2.6 and 37 degrees C. Although the residues of the E-F loop (residues, 86-89) have the highest crystallographic B-factors, the conformation of, this loop is reasonably well defined by the NMR data, and its backbone is, not especially mobile on the pico- to nanosecond time scale. Several, residues (Ser21, Lys60, Ala67, Leu87, and Glu112) exhibit large ratios of, T(1) to T(2), consistent with conformational exchange on a micro- to, millisecond time scale. The positions of these residues in the 3D, structure of beta-lactoglobulin are consistent with a role in modulating, access to the hydrophobic cavity.
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<StructureSection load='1dv9' size='340' side='right'caption='[[1dv9]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1dv9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DV9 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">Solution NMR</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=1dv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dv9 OCA], [https://pdbe.org/1dv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dv9 RCSB], [https://www.ebi.ac.uk/pdbsum/1dv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dv9 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/dv/1dv9_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=1dv9 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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1DV9 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=1DV9 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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Structural changes accompanying pH-induced dissociation of the beta-lactoglobulin dimer., Uhrinova S, Smith MH, Jameson GB, Uhrin D, Sawyer L, Barlow PN, Biochemistry. 2000 Apr 4;39(13):3565-74. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10736155 10736155]
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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: Barlow, P.N.]]
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[[Category: Barlow PN]]
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[[Category: Jameson, G.B.]]
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[[Category: Jameson GB]]
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[[Category: Sawyer, L.]]
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[[Category: Sawyer L]]
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[[Category: Smith, M.H.]]
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[[Category: Smith MH]]
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[[Category: Uhrin, D.]]
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[[Category: Uhrin D]]
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[[Category: Uhrinova, S.]]
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[[Category: Uhrinova S]]
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[[Category: beta-barrel]]
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[[Category: beta-lactoglobulin]]
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[[Category: low ph structure]]
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[[Category: triple resonance experiments]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:36:55 2007''
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Current revision

STRUCTURAL CHANGES ACCOMPANYING PH-INDUCED DISSOCIATION OF THE B-LACTOGLOBULIN DIMER

PDB ID 1dv9

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