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1dv9
From Proteopedia
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[[Image:1dv9.gif|left|200px]] | [[Image:1dv9.gif|left|200px]] | ||
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'''STRUCTURAL CHANGES ACCOMPANYING PH-INDUCED DISSOCIATION OF THE B-LACTOGLOBULIN DIMER''' | '''STRUCTURAL CHANGES ACCOMPANYING PH-INDUCED DISSOCIATION OF THE B-LACTOGLOBULIN DIMER''' | ||
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[[Category: Uhrin, D.]] | [[Category: Uhrin, D.]] | ||
[[Category: Uhrinova, S.]] | [[Category: Uhrinova, S.]] | ||
| - | [[Category: | + | [[Category: Beta-barrel]] |
| - | [[Category: | + | [[Category: Beta-lactoglobulin]] |
| - | [[Category: | + | [[Category: Low ph structure]] |
| - | [[Category: | + | [[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 | + | |
Revision as of 11:19, 2 May 2008
STRUCTURAL CHANGES ACCOMPANYING PH-INDUCED DISSOCIATION OF THE B-LACTOGLOBULIN DIMER
Overview
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 Structure
1DV9 is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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
