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| - | [[Image:1beb.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1beb| PDB=1beb | SCENE= }} | | {{STRUCTURE_1beb| PDB=1beb | SCENE= }} |
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| - | '''BOVINE BETA-LACTOGLOBULIN, LATTICE X'''
| + | ===BOVINE BETA-LACTOGLOBULIN, LATTICE X=== |
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| - | ==Overview==
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| - | BACKGROUND: beta-Lactoglobulin (beta-Lg) is the major whey protein in the milk of ruminants and many other mammals. Its function is not known, but it undergoes at least two pH-dependent conformational changes which may be important. Bovine beta-Lg crystallizes in several different lattices, and medium-resolution structures of orthorhombic lattice Y and trigonal lattice Z have been published. Triclinic lattice X and lattice Z crystals grow at pH values either side of the pH at which one of the pH-induced conformational changes occurs. A full understanding of the structure is needed to help explain both the conformational changes and the different denaturation behaviour of the genetic variants. RESULTS: We have redetermined the structure of beta-Lg lattice Z at 3.0 A resolution by multiple isomorphous replacement and have partially refined it (R factor = 24.8%). Using the dimer from this lattice Z structure as a search model, the triclinic crystal form grown at pH 6.5 (lattice X) has been solved by molecular replacement. Refinement of lattice X at 1.8 A resolution gave an R factor of 18.1%. The structure we have determined differs from previously published structures in several ways. CONCLUSIONS: Incorrect threading of the sequence in the published structures of beta-Lg affects four of the nine beta strands. The basic lipocalin fold of the polypeptide chain is unchanged, however. The relative orientation of the monomers in the beta-Lg dimer differs in the two lattices. On raising the pH, there is a rotation of approximately 5 degrees, which breaks a number of intersubunit hydrogen bonds. It is not yet clear, however, why the stability of the structure should depend so heavily upon the external loop around residue 64 or the beta strand with the free thiol, each of which shows genetic variation.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9115437}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9115437 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9115437}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Milk whey protein]] | | [[Category: Milk whey protein]] |
| | [[Category: Retinol-binding]] | | [[Category: Retinol-binding]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:24:12 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 18:58:01 2008'' |
Revision as of 15:58, 30 June 2008
Template:STRUCTURE 1beb
BOVINE BETA-LACTOGLOBULIN, LATTICE X
Template:ABSTRACT PUBMED 9115437
About this Structure
1BEB is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
Bovine beta-lactoglobulin at 1.8 A resolution--still an enigmatic lipocalin., Brownlow S, Morais Cabral JH, Cooper R, Flower DR, Yewdall SJ, Polikarpov I, North AC, Sawyer L, Structure. 1997 Apr 15;5(4):481-95. PMID:9115437
Page seeded by OCA on Mon Jun 30 18:58:01 2008
