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5efd

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<StructureSection load='5efd' size='340' side='right'caption='[[5efd]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
<StructureSection load='5efd' size='340' side='right'caption='[[5efd]], [[Resolution|resolution]] 1.67&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5efd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._ng-27 Bacillus sp. ng-27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EFD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EFD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5efd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._NG-27 Bacillus sp. NG-27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EFD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EFD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.674&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[5eb8|5eb8]], [[5eba|5eba]], [[5ebf|5ebf]]</div></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Endo-1,4-beta-xylanase Endo-1,4-beta-xylanase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.8 3.2.1.8] </span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5efd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5efd OCA], [https://pdbe.org/5efd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5efd RCSB], [https://www.ebi.ac.uk/pdbsum/5efd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5efd 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=5efd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5efd OCA], [https://pdbe.org/5efd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5efd RCSB], [https://www.ebi.ac.uk/pdbsum/5efd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5efd ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/O30700_9BACI O30700_9BACI]
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Cryptic pockets are visible in ligand-bound protein structures but are occluded in unbound structures. Utilizing these pockets in fragment-based drug-design provides an attractive option for proteins not tractable by classical binding sites. However, owing to their hidden nature, they are difficult to identify. Here, we show that small glycols find cryptic pockets on a diverse set of proteins. Initial crystallography experiments serendipitously revealed the ability of ethylene glycol, a small glycol, to identify a cryptic pocket on the W6A mutant of the RBSX protein (RBSX-W6A). Explicit-solvent molecular dynamics (MD) simulations of RBSX-W6A with the exposed state of the cryptic pocket (ethylene glycol removed) revealed closure of the pocket reiterating that the exposed state of cryptic pockets in general are unstable in the absence of ligands. Also, no change in the pocket was observed for simulations of RBSX-W6A with the occluded state of the cryptic pocket, suggesting that water molecules are not able to open the cryptic pocket. "Cryptic-pocket finding" potential of small glycols was then supported and generalized through additional crystallography experiments, explicit-cosolvent MD simulations, and protein data set construction and analysis. The cryptic pocket on RBSX-W6A was found again upon repeating the crystallography experiments with another small glycol, propylene glycol. Use of ethylene glycol as a probe molecule in cosolvent MD simulations led to the enhanced sampling of the exposed state of experimentally observed cryptic sites on a test set of two proteins (Niemann-Pick C2, Interleukin-2). Further, analyses of protein structures with validated cryptic sites showed that ethylene glycol molecules bind to sites on proteins (Bcl-xL, G-actin, myosin II, and glutamate receptor 2), which become apparent upon binding of biologically relevant ligands. Our study thus suggests potential application of the small glycols in experimental and computational fragment-based approaches to identify cryptic pockets in apparently undruggable and/or difficult targets, making these proteins amenable to drug-design strategies.
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Small Glycols Discover Cryptic Pockets on Proteins for Fragment-Based Approaches.,Bansia H, Mahanta P, Yennawar NH, Ramakumar S J Chem Inf Model. 2021 Mar 22;61(3):1322-1333. doi: 10.1021/acs.jcim.0c01126., Epub 2021 Feb 11. PMID:33570386<ref>PMID:33570386</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5efd" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus sp. ng-27]]
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[[Category: Bacillus sp. NG-27]]
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[[Category: Endo-1,4-beta-xylanase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bhardwaj, A]]
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[[Category: Bhardwaj A]]
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[[Category: Mahanta, P]]
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[[Category: Mahanta P]]
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[[Category: Ramakumar, S]]
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[[Category: Ramakumar S]]
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[[Category: Reddy, V S]]
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[[Category: Reddy VS]]
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[[Category: Hydrolase]]
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[[Category: Mutant]]
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[[Category: Xylanase]]
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Current revision

Crystal structure of a surface pocket creating mutant (W6A) of an alkali thermostable GH10 xylanase from Bacillus sp. NG-27

PDB ID 5efd

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