View source for 5h42


==Crystal Structure of 1,2-beta-oligoglucan phosphorylase from Lachnoclostridium phytofermentans in complex with alpha-d-glucose-1-phosphate==
<StructureSection load='5h42' size='340' side='right'caption='[[5h42]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5h42]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lachnoclostridium_phytofermentans_ISDg Lachnoclostridium phytofermentans ISDg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5H42 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=G1P:ALPHA-D-GLUCOSE-1-PHOSPHATE'>G1P</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</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=5h42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h42 OCA], [https://pdbe.org/5h42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5h42 RCSB], [https://www.ebi.ac.uk/pdbsum/5h42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5h42 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A9KJS6_LACP7 A9KJS6_LACP7] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycoside phosphorylases catalyze the phosphorolysis of oligosaccharides into sugar phosphates. Recently, we found a novel phosphorylase acting on beta-1,2-glucooligosaccharides with degrees of polymerization of 3 or more (1,2-beta-oligoglucan phosphorylase, SOGP) in glycoside hydrolase family (GH) 94. Here, we characterized SOGP from Lachnoclostridium phytofermentans (LpSOGP) and determined its crystal structure. LpSOGP is a monomeric enzyme that contains a unique beta-sandwich domain (Ndom1) at its N-terminus. Unlike the dimeric GH94 enzymes possessing catalytic pockets at their dimer interface, LpSOGP has a catalytic pocket between Ndom1 and the catalytic domain. In the complex structure of LpSOGP with sophorose, sophorose binds at subsites +1 to +2. Notably, the Glc moiety at subsite +1 is flipped compared with the corresponding ligands in other GH94 enzymes. This inversion suggests the great distortion of the glycosidic bond between subsites -1 and +1, which is likely unfavorable for substrate binding. Compensation for this disadvantage at subsite +2 can be accounted for by the small distortion of the glycosidic bond in the sophorose molecule. Therefore, the binding mode at subsites +1 and +2 defines the substrate specificity of LpSOGP, which provides mechanistic insights into the substrate specificity of a phosphorylase acting on beta-1,2-glucooligosaccharides.

Mechanistic insight into the substrate specificity of 1,2-beta-oligoglucan phosphorylase from Lachnoclostridium phytofermentans.,Nakajima M, Tanaka N, Furukawa N, Nihira T, Kodutsumi Y, Takahashi Y, Sugimoto N, Miyanaga A, Fushinobu S, Taguchi H, Nakai H Sci Rep. 2017 Feb 15;7:42671. doi: 10.1038/srep42671. PMID:28198470<ref>PMID:28198470</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5h42" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Lachnoclostridium phytofermentans ISDg]]
[[Category: Large Structures]]
[[Category: Furukawa N]]
[[Category: Fushinobu S]]
[[Category: Kodutsumi Y]]
[[Category: Miyanaga A]]
[[Category: Nakai H]]
[[Category: Nakajima M]]
[[Category: Nihira T]]
[[Category: Sugimoto N]]
[[Category: Taguchi H]]
[[Category: Takahashi Y]]
[[Category: Tanaka N]]