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2qo6

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Current revision

Crystal structure of the glycine 55 arginine mutant of zebrafish liver bile acid-binding protein complexed with cholic acid

Structural highlights

2qo6 is a 1 chain structure with sequence from Danio rerio. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.9Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FA10A_DANRE Binds hydrophobic ligands, such as cholate, in the cytoplasm. May be involved in intracellular lipid transport (By similarity). Binds one cholate per subunit.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Capaldi S, Guariento M, Saccomani G, Fessas D, Perduca M, Monaco HL. A single amino acid mutation in zebrafish (Danio rerio) liver bile acid-binding protein can change the stoichiometry of ligand binding. J Biol Chem. 2007 Oct 19;282(42):31008-18. Epub 2007 Aug 1. PMID:17670743 doi:10.1074/jbc.M705399200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qo6"

@@ Line 3: / Line 3: @@
 <StructureSection load='2qo6' size='340' side='right'caption='[[2qo6]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2qo6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Brachidanio_rerio Brachidanio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QO6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2qo6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Danio_rerio Danio rerio]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QO6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2QO6 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2qo4|2qo4]], [[2qo5|2qo5]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CHD:CHOLIC+ACID'>CHD</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fabp10 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7955 Brachidanio rerio])</td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2qo6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qo6 OCA], [https://pdbe.org/2qo6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2qo6 RCSB], [https://www.ebi.ac.uk/pdbsum/2qo6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2qo6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/FA10A_DANRE FA10A_DANRE]] Binds hydrophobic ligands, such as cholate, in the cytoplasm. May be involved in intracellular lipid transport (By similarity). Binds one cholate per subunit.
+[https://www.uniprot.org/uniprot/FA10A_DANRE FA10A_DANRE] Binds hydrophobic ligands, such as cholate, in the cytoplasm. May be involved in intracellular lipid transport (By similarity). Binds one cholate per subunit.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 37: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Brachidanio rerio]]
+[[Category: Danio rerio]]
 [[Category: Large Structures]]
-[[Category: Capaldi, S]]
+[[Category: Capaldi S]]
-[[Category: Monaco, H L]]
+[[Category: Monaco HL]]
-[[Category: Perduca, M]]
+[[Category: Perduca M]]
-[[Category: Saccomani, G]]
+[[Category: Saccomani G]]
-[[Category: Babp]]
-[[Category: Bile acid]]
-[[Category: Cholate]]
-[[Category: Cholic acid]]
-[[Category: Fabp]]
-[[Category: Fatty acid-binding protein]]
-[[Category: G55r mutant]]
-[[Category: Lipid binding protein]]
-[[Category: Lipid-binding]]
-[[Category: Liver bile acid-binding protein]]
-[[Category: Transport]]

2qo6

From Proteopedia

Current revision

Crystal structure of the glycine 55 arginine mutant of zebrafish liver bile acid-binding protein complexed with cholic acid

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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