1ifb: Difference between revisions

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-[[Image:1ifb.jpg|left|200px]]
-<!--
+==REFINED APOPROTEIN STRUCTURE OF RAT INTESTINAL FATTY ACID BINDING PROTEIN PRODUCED IN ESCHERICHIA COLI==
-The line below this paragraph, containing "STRUCTURE_1ifb", creates the "Structure Box" on the page.
+<StructureSection load='1ifb' size='340' side='right'caption='[[1ifb]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
-{{STRUCTURE_1ifb|  PDB=1ifb  |  SCENE=  }}
+</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>
-'''REFINED APOPROTEIN STRUCTURE OF RAT INTESTINAL FATTY ACID BINDING PROTEIN PRODUCED IN ESCHERICHIA COLI'''
+==See Also==
+*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-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.
+[[Category: Large Structures]]
+[[Category: Rattus rattus]]
-==About this Structure==
+[[Category: Banaszak LJ]]
-IFB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IFB OCA].
+[[Category: Gordon JI]]
+[[Category: Sacchettini JC]]
-==Reference==
-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://www.ncbi.nlm.nih.gov/pubmed/2682622 2682622]
-[[Category: Rattus norvegicus]]
-[[Category: Single protein]]
-[[Category: Banaszak, L J.]]
-[[Category: Gordon, J I.]]
-[[Category: Sacchettini, J C.]]
-[[Category: Fatty acid-binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 19:56:31 2008''