View source for 5yne


==Crystal structure of Pullulanase from Klebsiella pneumoniae complex at 10 mM alpha-cyclodextrin==
<StructureSection load='5yne' size='340' side='right'caption='[[5yne]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5yne]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Klebsiella_pneumoniae Klebsiella pneumoniae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YNE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YNE 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]] 2.199&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PRD_900015:alpha-cyclodextrin'>PRD_900015</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=5yne FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yne OCA], [https://pdbe.org/5yne PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yne RCSB], [https://www.ebi.ac.uk/pdbsum/5yne PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yne ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/W9BQ28_KLEPN W9BQ28_KLEPN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Crystal structures of Klebsiella pneumoniae pullulanase (KPP) in complex with alpha-cyclodextrin (alpha-CD), beta-cyclodextrin (beta-CD) and gamma-cyclodextrin (gamma-CD) were refined at around 1.98-2.59 A resolution from data collected at SPring-8. In the structures of the complexes obtained with 1 mM alpha-CD or gamma-CD, one molecule of CD was found at carbohydrate-binding module 41 only (CBM41). In the structures of the complexes obtained with 1 mM beta-CD or with 10 mM alpha-CD or gamma-CD, two molecules of CD were found at CBM41 and in the active-site cleft, where the hydrophobic residue of Phe746 occupies the inside cavity of the CD rings. In contrast to alpha-CD and gamma-CD, one beta-CD molecule was found at the active site only in the presence of 0.1 mM beta-CD. These results were coincident with the solution experiments, which showed that beta-CD inhibits this enzyme more than a thousand times more potently than alpha-CD and gamma-CD. The strong inhibition of beta-CD is caused by the optimized interaction between beta-CD and the side chain of Phe746. The increased Ki values of the F746A mutant for beta-CD supported the importance of Phe746 in the strong interaction of pullulanase with beta-CD.

Elucidation of the mechanism of interaction between Klebsiella pneumoniae pullulanase and cyclodextrin.,Saka N, Iwamoto H, Malle D, Takahashi N, Mizutani K, Mikami B Acta Crystallogr D Struct Biol. 2018 Nov 1;74(Pt 11):1115-1123. doi:, 10.1107/S2059798318014523. Epub 2018 Oct 30. PMID:30387770<ref>PMID:30387770</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5yne" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Klebsiella pneumoniae]]
[[Category: Large Structures]]
[[Category: Iwamoto H]]
[[Category: Mikami B]]
[[Category: Mizutani K]]
[[Category: Saka N]]
[[Category: Takahashi N]]