7ec9: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7ec9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EC9 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7ec9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7EC9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7EC9 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NOJ:1-DEOXYNOJIRIMYCIN'>NOJ</scene></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]] 1.8Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NOJ:1-DEOXYNOJIRIMYCIN'>NOJ</scene></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=7ec9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ec9 OCA], [https://pdbe.org/7ec9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ec9 RCSB], [https://www.ebi.ac.uk/pdbsum/7ec9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ec9 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=7ec9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ec9 OCA], [https://pdbe.org/7ec9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ec9 RCSB], [https://www.ebi.ac.uk/pdbsum/7ec9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ec9 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q9X274_THEMA Q9X274_THEMA] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 7ec9" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7ec9" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Glucanase 3D structures|Glucanase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
Latest revision as of 19:50, 29 November 2023
Structure of the Thermotoga maritima Family 5 endo-glucanase in complex with 1-deoxynojiromycinStructure of the Thermotoga maritima Family 5 endo-glucanase in complex with 1-deoxynojiromycin
Structural highlights
FunctionPublication Abstract from PubMedTmCel5B is a lichenase belonging to glycoside hydrolase family 5 subfamily 36 (GH5_36). To gain insights into the active site of this subfamily which contains multifunctional endoglycanases, we determined the crystal structure of TmCel5B in complex with an iminosugar, 1-deoxynojiromycin (DNJ). DNJ is bound to the -1 subsite, making a network of non-covalent interactions with the acid/base residue Glu139, the nucleophile Glu259, and with other residues that are conserved across the GH5 family. The catalytic site displayed a Glu-Arg-Glu triad of the catalytic glutamates that is unique to the GH5_36 subfamily. Structural comparison of active sites of GH5_36 homologs revealed divergent residues and loop regions that are likely molecular determinants of homolog-specific properties. Furthermore, a comparative analysis of the binding modes of iminocyclitol complexes of GH5 homologs revealed the structural basis of their binding to GH5 glycosidases, in which the subsite binding location, the interactions of the ligand with specific conserved residues, and the electrostatic interactions of the catalytic glutamates with the ring nitrogen, are crucial. Structure of an iminosugar complex of a glycoside hydrolase family 5 lichenase provides insights into the active site.,Garg P, Manoj N Biochimie. 2022 Sep 6. pii: S0300-9084(22)00226-7. doi:, 10.1016/j.biochi.2022.09.001. PMID:36084911[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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