6f3o: Difference between revisions

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-'''Unreleased structure'''
-The entry 6f3o is ON HOLD  until Paper Publication
+==Crystal structure of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa complexed with adenine, K+ and Zn2+ cations==
+<StructureSection load='6f3o' size='340' side='right' caption='[[6f3o]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6f3o]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6F3O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6F3O 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>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenosylhomocysteinase Adenosylhomocysteinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.3.1.1 3.3.1.1] </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=6f3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6f3o OCA], [http://pdbe.org/6f3o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6f3o RCSB], [http://www.ebi.ac.uk/pdbsum/6f3o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6f3o ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/SAHH_PSEAE SAHH_PSEAE]] May play a key role in the regulation of the intracellular concentration of adenosylhomocysteine.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa (PaSAHase) coordinates one K(+) ion and one Zn(2+) ion in the substrate binding area. The cations affect the enzymatic activity and substrate binding but the molecular mechanisms of their action are unknown. Enzymatic and isothermal titration calorimetry studies demonstrated that the K(+) ions stimulate the highest activity and strongest ligand binding in comparison to other alkali cations, while the Zn(2+) ions inhibit the enzyme activity. PaSAHase was crystallized in the presence of adenine nucleosides and K(+) or Rb(+) ions. The crystal structures show that the alkali ion is coordinated in close proximity of the purine ring and a (23)Na NMR study showed that the monovalent cation coordination site is formed upon ligand binding. The cation, bound in the area of a molecular hinge, orders and accurately positions the amide group of Q65 residue to allow its interaction with the ligand. Moreover, binding of potassium is required to enable unique dynamic properties of the enzyme that ensure its maximum catalytic activity. The Zn(2+) ion is bound in the area of a molecular gate that regulates access to the active site. Zn(2+) coordination switches the gate to a shut state and arrests the enzyme in its closed, inactive conformation.
-Authors:
+Metal-cation regulation of enzyme dynamics is a key factor influencing the activity of S-adenosyl-L-homocysteine hydrolase from Pseudomonas aeruginosa.,Czyrko J, Sliwiak J, Imiolczyk B, Gdaniec Z, Jaskolski M, Brzezinski K Sci Rep. 2018 Jul 27;8(1):11334. doi: 10.1038/s41598-018-29535-y. PMID:30054521<ref>PMID:30054521</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6f3o" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Adenosylhomocysteinase]]
+[[Category: Brzezinski, K]]
+[[Category: Czyrko, J]]
+[[Category: Hydrolase]]
+[[Category: Regulation of sam-dependent methylation reaction]]