1ifb: Difference between revisions

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[[Image:1ifb.jpg|left|200px]]<br /><applet load="1ifb" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1ifb.jpg|left|200px]]<br /><applet load="1ifb" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1ifb, resolution 1.96Å" />

'''REFINED APOPROTEIN STRUCTURE OF RAT INTESTINAL FATTY ACID BINDING PROTEIN PRODUCED IN ESCHERICHIA COLI'''<br />

==Overview==

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.

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.

==About this Structure==

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].

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://oca.weizmann.ac.il/oca-bin/ocashort?id=1IFB OCA].

==Reference==

Line 13:

[[Category: Rattus norvegicus]]

[[Category: Single protein]]

[[Category: Banaszak, L.J.]]

[[Category: Banaszak, L J.]]

[[Category: Gordon, J.I.]]

[[Category: Gordon, J I.]]

[[Category: Sacchettini, J.C.]]

[[Category: Sacchettini, J C.]]

[[Category: fatty acid-binding protein]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 17~~:21:~~37 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:18 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1ifb.jpg|left|200px]]<br /><applet load="1ifb" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1ifb.jpg|left|200px]]<br /><applet load="1ifb" size="350" 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==
-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.
+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.
 ==About this Structure==
-IFB 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].
+IFB 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1IFB OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Rattus norvegicus]]
 [[Category: Single protein]]
-[[Category: Banaszak, L.J.]]
+[[Category: Banaszak, L J.]]
-[[Category: Gordon, J.I.]]
+[[Category: Gordon, J I.]]
-[[Category: Sacchettini, J.C.]]
+[[Category: Sacchettini, J C.]]
 [[Category: fatty acid-binding protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:21:37 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:18 2008''