5b6a
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of Pyridoxal Kinasefrom Pseudomonas Aeruginosa== | |
| + | <StructureSection load='5b6a' size='340' side='right' caption='[[5b6a]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5b6a]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B6A OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B6A FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pyridoxal_kinase Pyridoxal kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.35 2.7.1.35] </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=5b6a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b6a OCA], [http://pdbe.org/5b6a PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b6a RCSB], [http://www.ebi.ac.uk/pdbsum/5b6a PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b6a ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PDXY_PSEAE PDXY_PSEAE]] Pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate (PLP). Catalyzes the phosphorylation of pyridoxal to PLP. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Pyridoxal kinase is a ubiquitous enzyme essential for pyridoxal 5'-phosphate (PLP) homeostasis since PLP is required for the catalytic activity of a variety of PLP-dependent enzymes involved in amino acid, lipid, and sugar metabolism as well as neurotransmitter biosynthesis. Previously, two catalytic mechanisms were proposed with regard to Pdx kinases, in which either the aspartate or the cysteine residue is involved as a catalytic residue. Because the Pdx kinase of Pseudomonas aeruginosa (PaPdxK) contains both residues, the catalytic mechanism of PaPdxK remains elusive. To elucidate the substrate-recognition and catalytic mechanisms of PaPdxK, the crystal structure of PaPdxK was determined at a 2.0 A resolution. The PaPdxK structure possesses a channel that can accommodate substrates and a metallic cofactor. Our structure-based biochemical and mutational analyses in combination with modeling studies suggest that PaPdxK catalysis is mediated by an acid-base mechanism through the catalytic acid Asp225 and a helical dipole moment. | ||
| - | + | Crystal structure and catalytic mechanism of pyridoxal kinase from Pseudomonas aeruginosa.,Kim MI, Hong M Biochem Biophys Res Commun. 2016 Sep 9;478(1):300-6. doi:, 10.1016/j.bbrc.2016.07.007. Epub 2016 Jul 15. PMID:27425248<ref>PMID:27425248</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5b6a" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Pyridoxal kinase]] | ||
| + | [[Category: Hong, M]] | ||
| + | [[Category: Kim, M I]] | ||
| + | [[Category: Pdxk]] | ||
| + | [[Category: Pseudomonas aeruginosa]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 15:57, 10 August 2016
Structure of Pyridoxal Kinasefrom Pseudomonas Aeruginosa
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