1ifb: Difference between revisions
m Protected "1ifb" [edit=sysop:move=sysop] |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image: | ==REFINED APOPROTEIN STRUCTURE OF RAT INTESTINAL FATTY ACID BINDING PROTEIN PRODUCED IN ESCHERICHIA COLI== | ||
<StructureSection load='1ifb' size='340' side='right' caption='[[1ifb]], [[Resolution|resolution]] 1.96Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1ifb]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IFB FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ifb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ifb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ifb RCSB], [http://www.ebi.ac.uk/pdbsum/1ifb PDBsum]</span></td></tr> | |||
<table> | |||
== 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/chain_selection.php?pdb_ID=2ata ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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:2682622<ref>PMID:2682622</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | |||
*[[Fatty acid-binding protein|Fatty acid-binding protein]] | |||
== | == References == | ||
[[ | <references/> | ||
__TOC__ | |||
== | </StructureSection> | ||
< | |||
[[Category: Rattus rattus]] | [[Category: Rattus rattus]] | ||
[[Category: Banaszak, L J.]] | [[Category: Banaszak, L J.]] | ||
Revision as of 11:39, 28 September 2014
REFINED APOPROTEIN STRUCTURE OF RAT INTESTINAL FATTY ACID BINDING PROTEIN PRODUCED IN ESCHERICHIA COLIREFINED APOPROTEIN STRUCTURE OF RAT INTESTINAL FATTY ACID BINDING PROTEIN PRODUCED IN ESCHERICHIA COLI
Structural highlights
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 PubMedRat 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. 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:2682622[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||