1p6p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1p6p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p6p, resolution 2.5&Aring;" /> '''Crystal Structure of ...)
Line 1: Line 1:
-
[[Image:1p6p.jpg|left|200px]]<br /><applet load="1p6p" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1p6p.jpg|left|200px]]<br /><applet load="1p6p" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1p6p, resolution 2.5&Aring;" />
caption="1p6p, resolution 2.5&Aring;" />
'''Crystal Structure of Toad Liver Basic Fatty Acid-Binding Protein'''<br />
'''Crystal Structure of Toad Liver Basic Fatty Acid-Binding Protein'''<br />
==Overview==
==Overview==
-
Two paralogous groups of fatty acid-binding proteins (FABPs) have been, described in vertebrate liver: liver FABP (L-FABP) type, extensively, characterized in mammals, and liver basic FABP (Lb-FABP) found in fish, amphibians, reptiles, and birds. We describe here the toad Lb-FABP, complete amino acid sequence, its X-ray structure to 2.5 A resolution, ligand-binding properties, and mechanism of fatty acid transfer to, phospholipid membranes. Alignment of the amino acid sequence of toad, Lb-FABP with known L-FABPs and Lb-FABPs shows that it is more closely, related to the other Lb-FABPs. Toad Lb-FABP conserves the 12, characteristic residues present in all Lb-FABPs and absent in L-FABPs and, presents the canonical fold characteristic of all the members of this, protein family. Eight out of the 12 conserved residues point to the, lipid-binding cavity of the molecule. In contrast, most of the 25 L-FABP, conserved residues are in clusters on the surface of the molecule. The, helix-turn-helix motif shows both a negative and positive electrostatic, potential surface as in rat L-FABP, and in contrast with the other FABP, types. The mechanism of anthroyloxy-labeled fatty acids transfer from, Lb-FABP to phospholipid membranes occurs by a diffusion-mediated process, as previously shown for L-FABP, but the rate of transfer is 1 order of, magnitude faster. Toad Lb-FABP can bind two cis-parinaric acid molecules, but only one trans-parinaric acid molecule while L-FABP binds two, molecules of both parinaric acid isomers. Although toad Lb-FABP shares, with L-FABP a broad ligand-binding specificity, the relative affinity is, different.
+
Two paralogous groups of fatty acid-binding proteins (FABPs) have been described in vertebrate liver: liver FABP (L-FABP) type, extensively characterized in mammals, and liver basic FABP (Lb-FABP) found in fish, amphibians, reptiles, and birds. We describe here the toad Lb-FABP complete amino acid sequence, its X-ray structure to 2.5 A resolution, ligand-binding properties, and mechanism of fatty acid transfer to phospholipid membranes. Alignment of the amino acid sequence of toad Lb-FABP with known L-FABPs and Lb-FABPs shows that it is more closely related to the other Lb-FABPs. Toad Lb-FABP conserves the 12 characteristic residues present in all Lb-FABPs and absent in L-FABPs and presents the canonical fold characteristic of all the members of this protein family. Eight out of the 12 conserved residues point to the lipid-binding cavity of the molecule. In contrast, most of the 25 L-FABP conserved residues are in clusters on the surface of the molecule. The helix-turn-helix motif shows both a negative and positive electrostatic potential surface as in rat L-FABP, and in contrast with the other FABP types. The mechanism of anthroyloxy-labeled fatty acids transfer from Lb-FABP to phospholipid membranes occurs by a diffusion-mediated process, as previously shown for L-FABP, but the rate of transfer is 1 order of magnitude faster. Toad Lb-FABP can bind two cis-parinaric acid molecules but only one trans-parinaric acid molecule while L-FABP binds two molecules of both parinaric acid isomers. Although toad Lb-FABP shares with L-FABP a broad ligand-binding specificity, the relative affinity is different.
==About this Structure==
==About this Structure==
-
1P6P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bufo_arenarum Bufo arenarum]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P6P OCA].
+
1P6P is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bufo_arenarum Bufo arenarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P6P OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Corsico, B.]]
[[Category: Corsico, B.]]
-
[[Category: Monaco, H.L.]]
+
[[Category: Monaco, H L.]]
[[Category: Perduca, M.]]
[[Category: Perduca, M.]]
-
[[Category: Pietro, S.M.Di.]]
+
[[Category: Pietro, S M.Di.]]
-
[[Category: Santome, J.A.]]
+
[[Category: Santome, J A.]]
[[Category: beta barrel]]
[[Category: beta barrel]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:31:36 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:47 2008''

Revision as of 12:25, 21 February 2008


1p6p, resolution 2.5Å

Drag the structure with the mouse to rotate

Crystal Structure of Toad Liver Basic Fatty Acid-Binding Protein

Overview

Two paralogous groups of fatty acid-binding proteins (FABPs) have been described in vertebrate liver: liver FABP (L-FABP) type, extensively characterized in mammals, and liver basic FABP (Lb-FABP) found in fish, amphibians, reptiles, and birds. We describe here the toad Lb-FABP complete amino acid sequence, its X-ray structure to 2.5 A resolution, ligand-binding properties, and mechanism of fatty acid transfer to phospholipid membranes. Alignment of the amino acid sequence of toad Lb-FABP with known L-FABPs and Lb-FABPs shows that it is more closely related to the other Lb-FABPs. Toad Lb-FABP conserves the 12 characteristic residues present in all Lb-FABPs and absent in L-FABPs and presents the canonical fold characteristic of all the members of this protein family. Eight out of the 12 conserved residues point to the lipid-binding cavity of the molecule. In contrast, most of the 25 L-FABP conserved residues are in clusters on the surface of the molecule. The helix-turn-helix motif shows both a negative and positive electrostatic potential surface as in rat L-FABP, and in contrast with the other FABP types. The mechanism of anthroyloxy-labeled fatty acids transfer from Lb-FABP to phospholipid membranes occurs by a diffusion-mediated process, as previously shown for L-FABP, but the rate of transfer is 1 order of magnitude faster. Toad Lb-FABP can bind two cis-parinaric acid molecules but only one trans-parinaric acid molecule while L-FABP binds two molecules of both parinaric acid isomers. Although toad Lb-FABP shares with L-FABP a broad ligand-binding specificity, the relative affinity is different.

About this Structure

1P6P is a Single protein structure of sequence from Bufo arenarum. Full crystallographic information is available from OCA.

Reference

Structural and biochemical characterization of toad liver fatty acid-binding protein., Di Pietro SM, Corsico B, Perduca M, Monaco HL, Santome JA, Biochemistry. 2003 Jul 15;42(27):8192-203. PMID:12846568

Page seeded by OCA on Thu Feb 21 14:25:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools