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| <StructureSection load='2wrz' size='340' side='right'caption='[[2wrz]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='2wrz' size='340' side='right'caption='[[2wrz]], [[Resolution|resolution]] 2.20Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[2wrz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WRZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WRZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2wrz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WRZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WRZ FirstGlance]. <br> |
- | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bap|1bap]], [[8abp|8abp]], [[1apb|1apb]], [[7abp|7abp]], [[6abp|6abp]], [[9abp|9abp]], [[5abp|5abp]], [[1abe|1abe]], [[1abf|1abf]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</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=2wrz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wrz OCA], [https://pdbe.org/2wrz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wrz RCSB], [https://www.ebi.ac.uk/pdbsum/2wrz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wrz 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=2wrz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wrz OCA], [https://pdbe.org/2wrz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wrz RCSB], [https://www.ebi.ac.uk/pdbsum/2wrz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wrz ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/ARAF_ECOLI ARAF_ECOLI]] Involved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction).
| + | [https://www.uniprot.org/uniprot/ARAF_ECOLI ARAF_ECOLI] Involved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction). |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Hocker, B]] | + | [[Category: Hocker B]] |
- | [[Category: Schreier, B]] | + | [[Category: Schreier B]] |
- | [[Category: Stumpp, C]] | + | [[Category: Stumpp C]] |
- | [[Category: Wiesner, S]] | + | [[Category: Wiesner S]] |
- | [[Category: Abp]]
| + | |
- | [[Category: Arabinose binding protein]]
| + | |
- | [[Category: Periplasm]]
| + | |
- | [[Category: Periplasmic binding protein]]
| + | |
- | [[Category: Receptor design]]
| + | |
- | [[Category: Sugar transport]]
| + | |
- | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
ARAF_ECOLI Involved in the high-affinity L-arabinose membrane transport system. Binds with high affinity to arabinose, but can also bind D-galactose (approximately 2-fold reduction) and D-fucose (approximately 40-fold reduction).
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
Computational design has been very successful in recent years: multiple novel ligand binding proteins as well as enzymes have been reported. We wanted to know in molecular detail how precise the predictions of the interactions of protein and ligands are. Therefore, we performed a structural analysis of a number of published receptors designed onto the periplasmic binding protein scaffold that were reported to bind to the new ligands with nano- to micromolar affinities. It turned out that most of these designed proteins are not suitable for structural studies due to instability and aggregation. However, we were able to solve the crystal structure of an arabinose binding protein designed to bind serotonin to 2.2 A resolution. While crystallized in the presence of an excess of serotonin, the protein is in an open conformation with no serotonin bound, although the side-chain conformations in the empty binding pocket are very similar to the conformations predicted. During subsequent characterization using isothermal titration calorimetry, CD, and NMR spectroscopy, no indication of binding could be detected for any of the tested designed receptors, whereas wild-type proteins bound their ligands as expected. We conclude that although the computational prediction of side-chain conformations appears to be working, it does not necessarily confer binding as expected. Hence, the computational design of ligand binding is not a solved problem and needs to be revisited.
Computational design of ligand binding is not a solved problem.,Schreier B, Stumpp C, Wiesner S, Hocker B Proc Natl Acad Sci U S A. 2009 Oct 15. PMID:19833875[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schreier B, Stumpp C, Wiesner S, Hocker B. Computational design of ligand binding is not a solved problem. Proc Natl Acad Sci U S A. 2009 Oct 15. PMID:19833875
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