Crystal structure of axolotl (<i>Ambystoma mexicanum</i>) liver bile acid‐binding protein bound to cholic and oleic acid

Capaldi, Stefano; Guariento, Mara; Perduca, Massimiliano; Pietro, Santiago M. Di; Santomé, J.A.; Monaco, Hugo L.

doi:10.1002/prot.20961

Cited by 16 publications

(17 citation statements)

References 51 publications

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“…somewhat smaller than the equivalent value for chicken L-BABP, 627.4 Å 3 (11), and axolotl L-BABP, 685.5 Å 3 (15)). All of these values are significantly larger that the value observed for the apo form of chicken L-BABP, 143.7 Å 3 (11).…”

Section: Structure and Ligand-binding Stoichiometry Of The Wild Typementioning

confidence: 70%

“…2 prompted us to design the G55R mutant of zebrafish L-BABP. The sequences of five L-BABPs are aligned in the figure, and the amino acids involved in ligand binding in the only two structures of co-crystals that were known, chicken (11) and axolotl (15), are indicated with white and black dots. Six amino acids participate in the binding in both species, and five (Tyr 14 , Thr 53 , Phe 96 , His 98 , and Gln 100 ) are conserved in all of the sequences.…”

Section: Structure and Ligand-binding Stoichiometry Of The Wild Typementioning

confidence: 99%

“…NMR and other biophysical techniques have also been used to study chicken L-BABP, which remains the best characterized member of the L-BABP family (16 -18). The most important result of these structural studies is that the stoichiometry of binding for cholate is of two ligands per protein molecule (11,15), whereas that for oleate is of only one molecule per binding site (15,17). It is an unusual characteristic of the paralogous L-FABPs that they bind two molecules of oleate in their binding sites (19,20).…”

mentioning

confidence: 99%

“…The first L-BABP three-dimensional structure determined by x-ray diffraction was that of chicken liver BABP (13), followed by toad (14) and axolotl L-BABP (15). NMR and other biophysical techniques have also been used to study chicken L-BABP, which remains the best characterized member of the L-BABP family (16 -18).…”

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confidence: 99%

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A Single Amino Acid Mutation in Zebrafish (Danio rerio) Liver Bile Acid-binding Protein Can Change the Stoichiometry of Ligand Binding

Capaldi

Guariento²,

Saccomani³

et al. 2007

Journal of Biological Chemistry

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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 threedimensional structure determination of zebrafish (Danio rerio) L-BABP to 1.5 Å 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 liver bile acid-binding proteins, formerly called liver "basic" fatty acid-binding proteins (FABPs), 2 belong to the conserved multigene family of the fatty acid-binding proteins (1-6). Originally, the different members of this family were named according to the tissue from which they were first isolated. More recently, an alternative nomenclature has been proposed, since it is well known that different FABP types can be present in the same tissue (7). In particular, in the liver of several vertebrates, two paralogous groups of FABPs have been described: the liver FABPs and another group that was initially called the liver "basic" FABPs and is currently referred to as the liver bile acid-binding proteins (L-BABPs) (8, 9). The reason for this unusual nomenclature was that the isoelectric point of the first protein of this group that was described, chicken liver BABP, is 9.0, and although it was evident that this protein was different from the canonical liver FABP, its specific ligand was unknown (10). When it was shown that this protein could specifically bind cholic acid, a change in its designation was suggested to avoid confusion (11). The cytosolic bile acid-binding proteins mediate the intracellular movement of bile acids to the membranes across which they exit or enter the cells via membrane-bound transporters (12). The L-BABPs have been shown to be present in birds, amphibians, reptiles, and fish but not in mammals that express the very similar ileal BABPs, formerly called gastrotropins. It is suspected, although not proved, that the function that they perform ...

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Section: Structure and Ligand-binding Stoichiometry Of The Wild Typementioning

confidence: 70%

Section: Structure and Ligand-binding Stoichiometry Of The Wild Typementioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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A Single Amino Acid Mutation in Zebrafish (Danio rerio) Liver Bile Acid-binding Protein Can Change the Stoichiometry of Ligand Binding

Capaldi

Guariento²,

Saccomani³

et al. 2007

Journal of Biological Chemistry

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“…So far, L-BABP has never been found in mammalian species, but it has been identified and characterized in some vertebrates including fish, amphibians, reptiles, and birds (Ceciliani et al, 1994;Di Pietro et al, 1996Córdoba et al, 1999;Denovan-Wright et al, 2000;Ko et al, 2004;Jordal et al, 2006). Recent research on the structure of the L-BABP crystal showed that the capacity of L-BABP for binding to long-chain fatty acids is weak, but is strong for bile acid (Schievano et al, 1994;Beringhelli et al, 2001;Guariento et al, 2008), which is consistent with the presumption that the main function of L-BABP is to transport bile acids rather than fatty acids in chicken (Nichesola et al, 2004;Capaldi et al, 2006).…”

Section: Introductionmentioning

confidence: 55%

Differential expression of L-FABP and L-BABP between fat and lean chickens

Zhang¹,

Shi²,

Liu³

et al. 2013

Genet. Mol. Res.

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ABSTRACT. Liver fatty acid-binding protein (L-FABP) and liver bile acid-binding protein (L-BABP), in the liver intra-cytoplasm of chicken, are members of the fatty acid-binding protein subfamily. This study was designed to analyze and compare L-FABP and L-BABP expression levels between fat and lean lines in chicken liver tissue, and to determine the relationship between their expression and lipid metabolism. Realtime polymerase chain reaction (PCR) and Western blotting were used to detect the mRNA and protein expression in liver tissue between the lean and fat lines. Real-time PCR showed that L-FABP mRNA expression in fat male chickens was higher than that in lean male chickens at 2, 3, 4, 5, 6, and 10 weeks of age (P < 0.05), and L-BABP mRNA expression in fat male chickens was higher than that in lean male chickens at 1, 2, 3, 4, 8, and 10 weeks of age (P < 0.05). Western blotting showed that the L-FABP protein expression in fat male chickens was higher than that in lean male chickens at 3, 5, 6, and 7 weeks of age (P < 0.05), and L-BABP protein expression in fat male chickens was higher than that in lean male chickens at 3, 4, 5, and 6 weeks of age (P < 0.05). These results suggested that chicken L-FABP and L-BABP affect abdominal fat deposition through differences in their expression level, and the possible Expression of chicken L-FABP and L-BABP mechanism is that a high expression level of L-FABP and L-BABP leads to a high lipogenesis rate and, ultimately, to lipid deposition.

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Review: The liver bile acid‐binding proteins

Monaco¹

2009

Biopolymers

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The liver bile acid-binding proteins, L-BABPs, formerly called the liver "basic" fatty acid-binding proteins, are a subfamily of the fatty acid-binding proteins, FABPs. All the members of this protein group share the same fold: a 10 stranded beta barrel in which two short helices are inserted in between the first and the second strand of antiparallel beta sheet. The barrel encloses the ligand binding cavity of the protein while the two helices are believed to be involved in ligand accessibility to the binding site. The L-BABP subfamily has been found to be present in the liver of several vertebrates: fish, amphibians, reptiles, and birds but not in mammals. The members of the FABP family present in mammals that appear to be more closely related to the L-BABPs are the liver FABPs and the ileal BABPs, both very extensively studied. Several L-BABP X-ray structures are available and chicken L-BABP has also been studied using NMR spectroscopy. The stoichiometry of ligand binding for bile acids, first determined by X-ray crystallography for the chicken liver protein, is of two cholates per protein molecule with the only exception of zebrafish L-BABP which, due to the presence of a disulfide bridge, has a stoichiometry of 1:1. The stoichiometry of ligand binding for fatty acids, determined with several different techniques, is 1:1. An unanswered question of great relevance is the identity of the protein that in mammals performs the function that in other vertebrates is carried out by the L-BABPS.

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Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid‐binding protein bound to cholic and oleic acid

Cited by 16 publications

References 51 publications

A Single Amino Acid Mutation in Zebrafish (Danio rerio) Liver Bile Acid-binding Protein Can Change the Stoichiometry of Ligand Binding

A Single Amino Acid Mutation in Zebrafish (Danio rerio) Liver Bile Acid-binding Protein Can Change the Stoichiometry of Ligand Binding

Differential expression of L-FABP and L-BABP between fat and lean chickens

Review: The liver bile acid‐binding proteins

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