1dv9: Difference between revisions

Revision as of 14:19, 2 May 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1DV9 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.

ReferenceReference

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:10736155 Page seeded by OCA on Fri May 2 14:19:22 2008

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OCA

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 [[Image:1dv9.gif|left|200px]]
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-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dv9 OCA], [http://www.ebi.ac.uk/pdbsum/1dv9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dv9 RCSB]</span>
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 '''STRUCTURAL CHANGES ACCOMPANYING PH-INDUCED DISSOCIATION OF THE B-LACTOGLOBULIN DIMER'''
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 [[Category: Uhrin, D.]]
 [[Category: Uhrinova, S.]]
-[[Category: beta-barrel]]
+[[Category: Beta-barrel]]
-[[Category: beta-lactoglobulin]]
+[[Category: Beta-lactoglobulin]]
-[[Category: low ph structure]]
+[[Category: Low ph structure]]
-[[Category: triple resonance experiment]]
+[[Category: Triple resonance experiment]]
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:19:22 2008''
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:49:29 2008''