1bwy: Difference between revisions

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-[[Image:1bwy.jpg|left|200px]]<br /><applet load="1bwy" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1bwy" />
-'''NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN'''<br />
-==Overview==
+==NMR STUDY OF BOVINE HEART FATTY ACID BINDING PROTEIN==
-The three-dimensional structure of the holo form of recombinant cellular bovine heart fatty-acid-binding protein (H-FABPc), a polypeptide of 133 amino acid residues with a molecular mass of 15 kDa, has been determined by multidimensional homonuclear and heteronuclear NMR spectroscopy applied to uniformly 15N-labeled and unlabeled protein. A nearly complete set of 1H and 15N chemical shift assignments was obtained. A total of 2329 intramolecular distance constraints and 42 side-chain chi 1 dihedral-angle constraints were derived from cross-relaxation and J coupling information. 3D nuclear Overhauser enhancement and exchange spectroscopy combined with heteronuclear multiple-quantum coherence (NOESY-HMQC) experiments, performed on a sample of uniformly 13C-labeled palmitic acid bound to unlabeled cellular heart fatty-acid-binding protein revealed 10 intermolecular contacts that determine the orientation of the bound fatty acid. An ensemble of protein conformations was calculated with the distance-geometry algorithm for NMR applications (DIANA) using the redundant dihedral-angle constraint (REDAC) strategy. After docking the fatty acid into the protein, the protein-ligand arrangement was subject to distance-restrained energy minimization. The overall conformation of the protein is a beta-barrel consisting of 10 antiparallel beta-strands which form two nearly orthogonal beta-sheets of five strands each. Two short helices form a helix-turn-helix motif in the N-terminal region of the polypeptide chain. The palmitic acid is bound within the protein in a U-shaped conformation close to the two helices. The obtained solution structure of the protein is consistent with a number of fatty-acid-binding-protein crystal structures.
+<StructureSection load='1bwy' size='340' side='right'caption='[[1bwy]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1bwy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BWY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BWY FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1bwy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bwy OCA], [https://pdbe.org/1bwy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bwy RCSB], [https://www.ebi.ac.uk/pdbsum/1bwy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bwy ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FABPH_BOVIN FABPH_BOVIN] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters.  MDGI reversibly inhibits proliferation of mammary carcinoma cells.
+== 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/bw/1bwy_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=1bwy ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-BWY is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BWY OCA].
+*[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Three-dimensional structure of bovine heart fatty-acid-binding protein with bound palmitic acid, determined by multidimensional NMR spectroscopy., Lassen D, Lucke C, Kveder M, Mesgarzadeh A, Schmidt JM, Specht B, Lezius A, Spener F, Ruterjans H, Eur J Biochem. 1995 May 15;230(1):266-80. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7601110 7601110]
 [[Category: Bos taurus]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Kveder, M.]]
+[[Category: Kveder M]]
-[[Category: Lassen, D.]]
+[[Category: Lassen D]]
-[[Category: Lezius, A.]]
+[[Category: Lezius A]]
-[[Category: Luecke, C.]]
+[[Category: Luecke C]]
-[[Category: Mesgarzadeh, A.]]
+[[Category: Mesgarzadeh A]]
-[[Category: Rueterjans, H.]]
+[[Category: Rueterjans H]]
-[[Category: Schmidt, J M.]]
+[[Category: Schmidt JM]]
-[[Category: Specht, B.]]
+[[Category: Specht B]]
-[[Category: Spener, F.]]
+[[Category: Spener F]]
-[[Category: fatty acid binding]]
-[[Category: fatty acid binding protein]]
-[[Category: heart muscle]]
-[[Category: intracellular lipid binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:08 2008''