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New page: left|200px<br /><applet load="1ifb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ifb, resolution 1.96Å" /> '''REFINED APOPROTEIN S...
 
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[[Image:1ifb.jpg|left|200px]]<br /><applet load="1ifb" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ifb, resolution 1.96&Aring;" />
'''REFINED APOPROTEIN STRUCTURE OF RAT INTESTINAL FATTY ACID BINDING PROTEIN PRODUCED IN ESCHERICHIA COLI'''<br />


==Overview==
==REFINED APOPROTEIN STRUCTURE OF RAT INTESTINAL FATTY ACID BINDING PROTEIN PRODUCED IN ESCHERICHIA COLI==
Rat intestinal fatty acid binding protein (I-FABP) is a member of a family, of cytoplasmic hydrophobic ligand-binding proteins. To gain insights about, the contribution of bound fatty acid to I-FABP's conformation and, mechanism of ligand binding, we have determined the structure of, Escherichia coli-derived rat apo-I-FABP to 1.96-A resolution and compared, it to the recently refined structure of I-FABP with bound palmitate. Both, apo- and holo-I-FABP are composed primarily of anti-parallel beta-strands, which form two nearly orthogonal beta-sheets ("beta-clam"). The overall, structures of the apo- and holo-I-FABP are nearly identical, with a root, mean square (rms) difference of 0.37 A between C alpha atoms, 0.38 A, between all main-chain atoms, and 0.94 A between all side-chain atoms., However, rms differences of greater than 1.3 A were noted for the side, chains of Ile-23, Lys-27, Arg-56, Leu-72, Ala-73, and Asp-74. The space, occupied by bound ligand in the core of the holoprotein is occupied in the, apo-protein by ordered solvent molecules. This results in an increase in, the total number of internal ordered solvent molecules from 7 in the, holoprotein to 13 in apo-I-FABP. This finding, together with observed, differences in the side-chain orientations of two residues (Arg-56 and, Lys-27) situated over a potential opening to the cores of the apo- and, holoproteins, suggests that solvent molecules play a critical role in, ligand binding. Moreover, the data indicate that the beta-clam structure, is stable even in the absence of bound ligand.
<StructureSection load='1ifb' size='340' side='right'caption='[[1ifb]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1ifb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IFB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IFB 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]] 1.96&#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=1ifb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ifb OCA], [https://pdbe.org/1ifb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ifb RCSB], [https://www.ebi.ac.uk/pdbsum/1ifb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ifb ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FABPI_RAT FABPI_RAT] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor (By similarity).
== 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/if/1ifb_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=1ifb ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1IFB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IFB OCA].
*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli., Sacchettini JC, Gordon JI, Banaszak LJ, Proc Natl Acad Sci U S A. 1989 Oct;86(20):7736-40. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2682622 2682622]
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus rattus]]
[[Category: Single protein]]
[[Category: Banaszak LJ]]
[[Category: Banaszak, L.J.]]
[[Category: Gordon JI]]
[[Category: Gordon, J.I.]]
[[Category: Sacchettini JC]]
[[Category: Sacchettini, J.C.]]
[[Category: fatty acid-binding protein]]
 
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Retrieved from "https://proteopedia.org/1ifb"