2blg

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STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 8.2

Structural highlights

2blg is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.46Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

LACB_BOVIN Primary component of whey, it binds retinol and is probably involved in the transport of that molecule.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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See Also

References

  1. Qin BY, Bewley MC, Creamer LK, Baker HM, Baker EN, Jameson GB. Structural basis of the Tanford transition of bovine beta-lactoglobulin. Biochemistry. 1998 Oct 6;37(40):14014-23. PMID:9760236 doi:10.1021/bi981016t

Contents


PDB ID 2blg

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