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| - | [[Image:2qo4.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2qo4| PDB=2qo4 | SCENE= }} | | {{STRUCTURE_2qo4| PDB=2qo4 | SCENE= }} |
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| - | '''Crystal structure of zebrafish liver bile acid-binding protein complexed with cholic acid'''
| + | ===Crystal structure of zebrafish liver bile acid-binding protein complexed with cholic acid=== |
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| - | ==Overview==
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| - | In all of the liver bile acid-binding proteins (L-BABPs) studied so far, it has been found that the stoichiometry of binding is of two cholate molecules per internal binding site. In this paper, we describe the expression, purification, crystallization, and three-dimensional structure determination of zebrafish (Danio rerio) L-BABP to 1.5A resolution, which is currently the highest available for a protein of this family. Since we have found that in zebrafish, the stoichiometry of binding in the protein cavity is of only one cholate molecule per wild type L-BABP, we examined the role of two crucial amino acids present in the binding site. Using site-directed mutagenesis, we have prepared, crystallized, and determined the three-dimensional structure of co-crystals of two mutants. The mutant G55R has the same stoichiometry of binding as the wild type protein, whereas the C91T mutant changes the stoichiometry of binding from one to two ligand molecules in the cavity and therefore appears to be more similar to the other members of the L-BABP family. Based on the presence or absence of a single disulfide bridge, it can be postulated that fish should bind a single cholate molecule, whereas amphibians and higher vertebrates should bind two. Isothermal titration calorimetry has also revealed the presence in the wild type protein and the G55R mutant of an additional binding site, different from the first and probably located on the surface of the molecule.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17670743}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17670743 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17670743}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Liver bile acid-binding protein]] | | [[Category: Liver bile acid-binding protein]] |
| | [[Category: Transport]] | | [[Category: Transport]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 15:16:59 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:26:42 2008'' |
Revision as of 12:26, 27 July 2008
Template:STRUCTURE 2qo4
Crystal structure of zebrafish liver bile acid-binding protein complexed with cholic acid
Template:ABSTRACT PUBMED 17670743
About this Structure
2QO4 is a Single protein structure of sequence from Danio rerio. Full crystallographic information is available from OCA.
Reference
A single amino acid mutation in zebrafish (Danio rerio) liver bile acid-binding protein can change the stoichiometry of ligand binding., Capaldi S, Guariento M, Saccomani G, Fessas D, Perduca M, Monaco HL, J Biol Chem. 2007 Oct 19;282(42):31008-18. Epub 2007 Aug 1. PMID:17670743
Page seeded by OCA on Sun Jul 27 15:26:42 2008
