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| | ==NMR Solution Structure of the Engineered Lipocalin FluA(R95K) Northeast Structural Genomics Target OR17== | | ==NMR Solution Structure of the Engineered Lipocalin FluA(R95K) Northeast Structural Genomics Target OR17== |
| - | <StructureSection load='1t0v' size='340' side='right' caption='[[1t0v]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='1t0v' size='340' side='right'caption='[[1t0v]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1t0v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Large_white_butterfly Large white butterfly]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T0V FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1t0v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pieris_brassicae Pieris brassicae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T0V FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1n0s|1n0s]], [[1bbp|1bbp]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=1t0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0v OCA], [http://pdbe.org/1t0v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t0v RCSB], [http://www.ebi.ac.uk/pdbsum/1t0v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0v 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=1t0v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0v OCA], [https://pdbe.org/1t0v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t0v RCSB], [https://www.ebi.ac.uk/pdbsum/1t0v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t0v ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BBP_PIEBR BBP_PIEBR]] This protein binds the blue pigments bilins.<ref>PMID:3202956</ref> | + | [https://www.uniprot.org/uniprot/BBP_PIEBR BBP_PIEBR] This protein binds the blue pigments bilins.<ref>PMID:3202956</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t0/1t0v_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t0/1t0v_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Large white butterfly]] | + | [[Category: Large Structures]] |
| - | [[Category: Liu, G]]
| + | |
| - | [[Category: Mills, J L]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Skerra, A]]
| + | |
| - | [[Category: Szyperski, T]]
| + | |
| - | [[Category: Anticalin]]
| + | |
| - | [[Category: Beta-barrel]]
| + | |
| - | [[Category: Ligand binding protein]]
| + | |
| - | [[Category: Lipocalin]]
| + | |
| - | [[Category: Nesg]]
| + | |
| | [[Category: Pieris brassicae]] | | [[Category: Pieris brassicae]] |
| - | [[Category: Protein engineering]] | + | [[Category: Liu G]] |
| - | [[Category: PSI, Protein structure initiative]] | + | [[Category: Mills JL]] |
| | + | [[Category: Skerra A]] |
| | + | [[Category: Szyperski T]] |
| Structural highlights
Function
BBP_PIEBR This protein binds the blue pigments bilins.[1]
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
The NMR structure of the 21 kDa lipocalin FluA, which was previously obtained by combinatorial design, elucidates a reshaped binding site specific for the dye fluorescein resulting from 21 side chain replacements with respect to the parental lipocalin, the naturally occurring bilin-binding protein (BBP). As expected, FluA exhibits the lipocalin fold of BBP, comprising eight antiparallel beta-strands forming a beta-barrel with an alpha-helix attached to its side. Comparison of the NMR structure of free FluA with the X-ray structures of BBP.biliverdin IX(gamma) and FluA.fluorescein complexes revealed significant conformational changes in the binding pocket, which is formed by four loops at the open end of the beta-barrel as well as adjoining beta-strand segments. An "induced fit" became apparent for the side chain conformations of Arg 88 and Phe 99, which contact the bound fluorescein in the complex and undergo concerted rearrangement upon ligand binding. Moreover, slower internal motional modes of the polypeptide backbone were identified by measuring transverse (15)N backbone spin relaxation times in the rotating frame for free FluA and also for the FluA.fluorescein complex. A reduction in the level of such motions was detected upon complex formation, indicating rigidification of the protein structure and loss of conformational entropy. This hypothesis was confirmed by isothermal titration calorimetry, showing that ligand binding is enthalpy-driven, thus overcompensating for the negative entropy associated with both ligand binding per se and rigidification of the protein. Our investigation of the solution structure and dynamics as well as thermodynamics of lipocalin-ligand interaction not only provides insight into the general mechanism of small molecule accommodation in the deep and narrow cavity of this abundant class of proteins but also supports the future design of corresponding binding proteins with novel specificities, so-called "anticalins".
NMR structure and dynamics of the engineered fluorescein-binding lipocalin FluA reveal rigidification of beta-barrel and variable loops upon enthalpy-driven ligand binding.,Mills JL, Liu G, Skerra A, Szyperski T Biochemistry. 2009 Aug 11;48(31):7411-9. PMID:19603796[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Suter F, Kayser H, Zuber H. The complete amino-acid sequence of the bilin-binding protein from Pieris brassicae and its similarity to a family of serum transport proteins like the retinol-binding proteins. Biol Chem Hoppe Seyler. 1988 Jun;369(6):497-505. PMID:3202956
- ↑ Mills JL, Liu G, Skerra A, Szyperski T. NMR structure and dynamics of the engineered fluorescein-binding lipocalin FluA reveal rigidification of beta-barrel and variable loops upon enthalpy-driven ligand binding. Biochemistry. 2009 Aug 11;48(31):7411-9. PMID:19603796 doi:10.1021/bi900535j
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