3wrf: Difference between revisions
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The | ==The crystal structure of native HypBA1 from Bifidobacterium longum JCM 1217== | ||
<StructureSection load='3wrf' size='340' side='right'caption='[[3wrf]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3wrf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bifidobacterium_longum_subsp._longum_JCM_1217 Bifidobacterium longum subsp. longum JCM 1217]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WRF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WRF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=3wrf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wrf OCA], [https://pdbe.org/3wrf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wrf RCSB], [https://www.ebi.ac.uk/pdbsum/3wrf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wrf ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/HYBA1_BIFL2 HYBA1_BIFL2] Beta-L-arabinofuranosidase that removes the beta-L-arabinofuranose residue from the non-reducing end of various substrates, including beta-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara-beta-1,2-Ara-beta-Hyp (Ara(2)-Hyp), Ara-beta-1,2-Ara-beta-1,2-Ara-beta-Hyp (Ara(3)-Hyp), and beta-L-arabinofuranosyl-(1->2)-1-O-methyl-beta-L-arabinofuranose. In the presence of 1-alkanols, shows transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bifidobacterium longum subsp. longum JCM 1217]] | |||
[[Category: Large Structures]] | |||
[[Category: Chan HC]] | |||
[[Category: Chen CC]] | |||
[[Category: Cheng YS]] | |||
[[Category: Guo RT]] | |||
[[Category: Ho MR]] | |||
[[Category: Hsu ST]] | |||
[[Category: Huang CH]] | |||
[[Category: Huang YN]] | |||
[[Category: Ko TP]] | |||
[[Category: Liu JR]] | |||
[[Category: Wang I]] | |||
[[Category: Zeng YF]] | |||
[[Category: Zhu Z]] |
Latest revision as of 13:35, 6 November 2024
The crystal structure of native HypBA1 from Bifidobacterium longum JCM 1217The crystal structure of native HypBA1 from Bifidobacterium longum JCM 1217
Structural highlights
FunctionHYBA1_BIFL2 Beta-L-arabinofuranosidase that removes the beta-L-arabinofuranose residue from the non-reducing end of various substrates, including beta-L-arabinofuranosyl-hydroxyproline (Ara-Hyp), Ara-beta-1,2-Ara-beta-Hyp (Ara(2)-Hyp), Ara-beta-1,2-Ara-beta-1,2-Ara-beta-Hyp (Ara(3)-Hyp), and beta-L-arabinofuranosyl-(1->2)-1-O-methyl-beta-L-arabinofuranose. In the presence of 1-alkanols, shows transglycosylation activity, retaining the anomeric configuration of the arabinofuranose residue. |
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