2blg | pdb_00002blg
STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 8.2
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| 2blg, resolution 2.46Å | |||||||||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
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.
About this Structure
2BLG is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 16:03:30 2008
