1bsy
From Proteopedia
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| - | [[Image:1bsy.gif|left|200px]] | + | [[Image:1bsy.gif|left|200px]] |
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| - | '''STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 7.1''' | + | {{Structure |
| + | |PDB= 1bsy |SIZE=350|CAPTION= <scene name='initialview01'>1bsy</scene>, resolution 2.24Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 7.1''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1BSY is a [ | + | 1BSY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BSY OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9760236 9760236] |
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transport]] | [[Category: transport]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:15:20 2008'' |
Revision as of 08:15, 20 March 2008
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| , resolution 2.24Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 7.1
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
1BSY 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
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