1s2d: Difference between revisions
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<StructureSection load='1s2d' size='340' side='right'caption='[[1s2d]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='1s2d' size='340' side='right'caption='[[1s2d]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1s2d]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1s2d]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_casei_e"_von_freudenreich_and_thoni_1904 "bacillus casei e" von freudenreich and thoni 1904]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S2D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S2D FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADE:ADENINE'>ADE</scene>, <scene name='pdbligand=V3M:2-deoxy-2-fluoro-alpha-D-arabinofuranose'>V3M</scene></td></tr> | ||
<tr id=' | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f8y|1f8y]], [[1s2g|1s2g]], [[1s2i|1s2i]], [[1s2l|1s2l]], [[1s3f|1s3f]]</div></td></tr> | ||
<tr id=' | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ptd, ndtA, ntd_1, BC335_1936, BCM45_08885, BDKNPLJD_00991, DM475_00825, GDZ32_10450, LH5_01102 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1587 "Bacillus casei e" von Freudenreich and Thoni 1904])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Nucleoside_deoxyribosyltransferase Nucleoside deoxyribosyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.6 2.4.2.6] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1s2d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s2d OCA], [https://pdbe.org/1s2d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s2d RCSB], [https://www.ebi.ac.uk/pdbsum/1s2d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s2d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == |
Revision as of 10:25, 22 September 2021
Purine 2'-Deoxyribosyl complex with arabinoside: Ribosylated Intermediate (AraA)Purine 2'-Deoxyribosyl complex with arabinoside: Ribosylated Intermediate (AraA)
Structural highlights
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 PubMedThe structure of class I N-deoxyribosyltransferase from Lactobacillus helveticus was determined by X-ray crystallography. Unlike class II N-deoxyribosyltransferases, which accept either purine or pyrimidine deoxynucleosides, class I enzymes are specific for purines as both the donor and acceptor base. Both class I and class II enzymes are highly specific for deoxynucleosides. The class I structure reveals similarities with the previously determined class II enzyme from Lactobacillus leichmanni [Armstrong, S. A., Cook, W. J., Short, S. A., and Ealick, S. E. (1996) Structure 4, 97-107]. The specificity of the class I enzyme for purine deoxynucleosides can be traced to a loop (residues 48-62), which shields the active site in the class II enzyme. In the class I enzyme, the purine base itself shields the active site from the solvent, while the smaller pyrimidine base cannot. The structure of the enzyme with a bound ribonucleoside shows that the nucleophilic oxygen atom of Glu101 hydrogen bonds to the O2' atom, rendering it unreactive and thus explaining the specificity for 2'-deoxynucleosides. The structure of a ribosylated enzyme intermediate reveals movements that occur during cleavage of the N-glycosidic bond. The structures of complexes with substrates and substrate analogues show that the purine base can bind in several different orientations, thus explaining the ability of the enzyme to catalyze alternate deoxyribosylation at the N3 or N7 position. Structures of purine 2'-deoxyribosyltransferase, substrate complexes, and the ribosylated enzyme intermediate at 2.0 A resolution.,Anand R, Kaminski PA, Ealick SE Biochemistry. 2004 Mar 9;43(9):2384-93. PMID:14992575[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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