5yn2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5yn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yn2 OCA], [http://pdbe.org/5yn2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yn2 RCSB], [http://www.ebi.ac.uk/pdbsum/5yn2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yn2 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5yn2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yn2 OCA], [http://pdbe.org/5yn2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yn2 RCSB], [http://www.ebi.ac.uk/pdbsum/5yn2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yn2 ProSAT]</span></td></tr>
</table>
</table>
 +
<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 5yn2" style="background-color:#fffaf0;"></div>
 +
== References ==
 +
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 08:53, 14 November 2018

Crystal structure of apo Pullulanase from Klebsiella pneumoniae in space group P43212

5yn2, resolution 2.30Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools