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2ftb

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

Structural highlights

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

Function

FABP2_AMBME Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity). The specificity of axolotl L-FABP differs from that of LB-FABP. Binds 2 ligands per protein molecule.

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

The family of the liver bile acid-binding proteins (L-BABPs), formerly called liver basic fatty acid-binding proteins (Lb-FABPs) shares fold and sequence similarity with the paralogous liver fatty acid-binding proteins (L-FABPs) but has a different stoichiometry and specificity of ligand binding. This article describes the first X-ray structure of a member of the L-BABP family, axolotl (Ambystoma mexicanum) L-BABP, bound to two different ligands: cholic and oleic acid. The protein binds one molecule of oleic acid in a position that is significantly different from that of either of the two molecules that bind to rat liver FABP. The stoichiometry of binding of cholate is of two ligands per protein molecule, as observed in chicken L-BABP. The cholate molecule that binds buried most deeply into the internal cavity overlaps well with the analogous bound to chicken L-BABP, whereas the second molecule, which interacts with the first only through hydrophobic contacts, is more external and exposed to the solvent.

Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic and oleic acid.,Capaldi S, Guariento M, Perduca M, Di Pietro SM, Santome JA, Monaco HL Proteins. 2006 Jul 1;64(1):79-88. PMID:16555310^[1]

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

References

↑ Capaldi S, Guariento M, Perduca M, Di Pietro SM, Santome JA, Monaco HL. Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to cholic and oleic acid. Proteins. 2006 Jul 1;64(1):79-88. PMID:16555310 doi:10.1002/prot.20961

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/2ftb"

@@ Line 1: / Line 1: @@
 ==Crystal structure of axolotl (Ambystoma mexicanum) liver bile acid-binding protein bound to oleic acid==
-<StructureSection load='2ftb' size='340' side='right' caption='[[2ftb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='2ftb' size='340' side='right'caption='[[2ftb]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ftb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ambystoma_mexicanum Ambystoma mexicanum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FTB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2FTB FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ftb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ambystoma_mexicanum Ambystoma mexicanum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FTB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FTB FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OLA:OLEIC+ACID'>OLA</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]] 2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2ft9|2ft9]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OLA:OLEIC+ACID'>OLA</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ftb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ftb OCA], [http://pdbe.org/2ftb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ftb RCSB], [http://www.ebi.ac.uk/pdbsum/2ftb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ftb ProSAT]</span></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=2ftb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ftb OCA], [https://pdbe.org/2ftb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ftb RCSB], [https://www.ebi.ac.uk/pdbsum/2ftb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ftb ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FABP2_AMBME FABP2_AMBME]] Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity). The specificity of axolotl L-FABP differs from that of LB-FABP. Binds 2 ligands per protein molecule.
+[https://www.uniprot.org/uniprot/FABP2_AMBME FABP2_AMBME] Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity). The specificity of axolotl L-FABP differs from that of LB-FABP. Binds 2 ligands per protein molecule.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[Fatty acid-binding protein|Fatty acid-binding protein]]
+*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
 == References ==
 <references/>
@@ Line 37: / Line 37: @@
 </StructureSection>
 [[Category: Ambystoma mexicanum]]
-[[Category: Capaldi, S]]
+[[Category: Large Structures]]
-[[Category: Guariento, M]]
+[[Category: Capaldi S]]
-[[Category: Monaco, H L]]
+[[Category: Di Pietro SM]]
-[[Category: Perduca, M]]
+[[Category: Guariento M]]
-[[Category: Pietro, S M.Di]]
+[[Category: Monaco HL]]
-[[Category: Santome, J A]]
+[[Category: Perduca M]]
-[[Category: Axolotl]]
+[[Category: Santome JA]]
-[[Category: Babp]]
-[[Category: Lb-fabp]]
-[[Category: Lipid binding protein]]
-[[Category: Liver basic fatty acid-binding protein]]
-[[Category: Liver bile acid-binding protein]]
-[[Category: Oleic acid]]

2ftb

From Proteopedia

Current revision

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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