This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1p6p

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:05, 14 February 2024) (edit) (undo)
 
(15 intermediate revisions not shown.)
Line 1: Line 1:
-
[[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;" />
 
-
'''Crystal Structure of Toad Liver Basic Fatty Acid-Binding Protein'''<br />
 
-
==Overview==
+
==Crystal Structure of Toad Liver Basic Fatty Acid-Binding Protein==
-
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.
+
<StructureSection load='1p6p' size='340' side='right'caption='[[1p6p]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1p6p]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhinella_arenarum Rhinella arenarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P6P FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</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=1p6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p6p OCA], [https://pdbe.org/1p6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p6p RCSB], [https://www.ebi.ac.uk/pdbsum/1p6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p6p ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/FABPL_RHIAE FABPL_RHIAE]
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p6/1p6p_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1p6p ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
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].
+
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12846568 12846568]
+
[[Category: Large Structures]]
-
[[Category: Bufo arenarum]]
+
[[Category: Rhinella arenarum]]
-
[[Category: Single protein]]
+
[[Category: Corsico B]]
-
[[Category: Corsico, B.]]
+
[[Category: Di Pietro SM]]
-
[[Category: Monaco, H L.]]
+
[[Category: Monaco HL]]
-
[[Category: Perduca, M.]]
+
[[Category: Perduca M]]
-
[[Category: Pietro, S M.Di.]]
+
[[Category: Santome JA]]
-
[[Category: Santome, J A.]]
+
-
[[Category: beta barrel]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:47 2008''
+

Current revision

Crystal Structure of Toad Liver Basic Fatty Acid-Binding Protein

PDB ID 1p6p

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools