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| | ==NMR structural analysis of apo chicken liver bile acid binding protein== | | ==NMR structural analysis of apo chicken liver bile acid binding protein== |
| - | <StructureSection load='1zry' size='340' side='right' caption='[[1zry]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='1zry' size='340' side='right'caption='[[1zry]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1zry]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZRY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZRY FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1zry]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZRY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZRY FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mvg|1mvg]], [[1tvq|1tvq]], [[1tw4|1tw4]]</td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zry OCA], [http://pdbe.org/1zry PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zry RCSB], [http://www.ebi.ac.uk/pdbsum/1zry PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zry ProSAT]</span></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=1zry FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zry OCA], [https://pdbe.org/1zry PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zry RCSB], [https://www.ebi.ac.uk/pdbsum/1zry PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zry ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FABPL_CHICK FABPL_CHICK]] Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. Binds 2 molecules of cholate per subunit. | + | [https://www.uniprot.org/uniprot/FABPL_CHICK FABPL_CHICK] Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. Binds 2 molecules of cholate per subunit. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </div> | | </div> |
| | <div class="pdbe-citations 1zry" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 1zry" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Fatty acid-binding protein 3D structures|Fatty acid-binding protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chick]] | + | [[Category: Gallus gallus]] |
| - | [[Category: Catalano, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Cicero, D]] | + | [[Category: Catalano M]] |
| - | [[Category: Eliseo, T]] | + | [[Category: Cicero D]] |
| - | [[Category: Fogolari, F]] | + | [[Category: Eliseo T]] |
| - | [[Category: Foote, J]] | + | [[Category: Fogolari F]] |
| - | [[Category: Luppi, M]] | + | [[Category: Foote J]] |
| - | [[Category: Molinari, H]] | + | [[Category: Luppi M]] |
| - | [[Category: Ragona, L]] | + | [[Category: Molinari H]] |
| - | [[Category: Zetta, L]] | + | [[Category: Ragona L]] |
| - | [[Category: Beta barrel]]
| + | [[Category: Zetta L]] |
| - | [[Category: Lipid binding protein]]
| + | |
| Structural highlights
Function
FABPL_CHICK Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport. Binds 2 molecules of cholate per subunit.
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 PubMed
Apo chicken liver bile acid-binding protein has been structurally characterized by NMR. The dynamic behavior of the protein in its apo- and holo-forms, complexed with chenodeoxycholate, has been determined via (15)N relaxation and steady state heteronuclear (15)N((1)H) nuclear Overhauser effect measurements. The dynamic parameters were obtained at two pH values (5.6 and 7.0) for the apoprotein and at pH 7.0 for the holoprotein, using the model free approach. Relaxation studies, performed at three different magnetic fields, revealed a substantial conformational flexibility on the microsecond to millisecond time scales, mainly localized in the C-terminal face of the beta-barrel. The observed dynamics are primarily caused by the protonation/deprotonation of a buried histidine residue, His(98), located on this flexible face. A network of polar buried side chains, defining a spine going from the E to J strand, is likely to provide the long range connectivity needed to communicate motion from His(98) to the EF loop region. NMR data are accompanied by molecular dynamics simulations, suggesting that His(98) protonation equilibrium is the triggering event for the modulation of a functionally important motion, i.e. the opening/closing at the protein open end, whereas ligand binding stabilizes one of the preexisting conformations (the open form). The results presented here, complemented with an analysis of proteins belonging to the intracellular lipid-binding protein family, are consistent with a model of allosteric activation governing the binding mechanism. The functional role of this mechanism is thoroughly discussed within the framework of the mechanism for the enterohepatic circulation of bile acids.
NMR dynamic studies suggest that allosteric activation regulates ligand binding in chicken liver bile acid-binding protein.,Ragona L, Catalano M, Luppi M, Cicero D, Eliseo T, Foote J, Fogolari F, Zetta L, Molinari H J Biol Chem. 2006 Apr 7;281(14):9697-709. Epub 2006 Jan 26. PMID:16439356[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ragona L, Catalano M, Luppi M, Cicero D, Eliseo T, Foote J, Fogolari F, Zetta L, Molinari H. NMR dynamic studies suggest that allosteric activation regulates ligand binding in chicken liver bile acid-binding protein. J Biol Chem. 2006 Apr 7;281(14):9697-709. Epub 2006 Jan 26. PMID:16439356 doi:10.1074/jbc.M513003200
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