2f7k

<StructureSection load='2f7k' size='340' side='right' caption='[[2f7k]], [[Resolution|resolution]] 2.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[2f7k]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F7K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2F7K FirstGlance]. <br>

</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=2f7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f7k OCA], [http://pdbe.org/2f7k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2f7k RCSB], [http://www.ebi.ac.uk/pdbsum/2f7k PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/PDXK_HUMAN PDXK_HUMAN]] Required for synthesis of pyridoxal-5-phosphate from vitamin B6.

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f7/2f7k_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

Pyridoxal kinase, a member of the ribokinase superfamily, catalyzes the ATP-dependent phosphorylation reaction of vitamin B6 and is an essential enzyme in the formation of pyridoxal-5'-phosphate, a key cofactor for over 100 enzymes. Pyridoxal kinase is thus regarded as a potential target for pharmacological agents. In this paper, we report the 2.8 angstroms crystal structure of human pyridoxal kinase (HPLK) expressed in Escherichia coli. The diffraction data revealed unexpected merohedral perfect twinning along the crystallographic c axis. Taking perfect twinning into account, the structure in dimeric form was well refined according to the CNS program. Structure comparison reveals that the key 12-residue peptide over the active site in HPLK is a beta-strand/loop/beta-strand flap, while the corresponding peptide in sheep brain enzyme adopts a loop conformation. Moreover, HPLK possesses a more hydrophobic ATP-binding pocket. This structure will facilitate further biochemical studies and structure-based design of drugs related to pyridoxal kinase.

Crystal structure of human pyridoxal kinase.,Cao P, Gong Y, Tang L, Leung YC, Jiang T J Struct Biol. 2006 Jun;154(3):327-32. Epub 2006 Mar 20. PMID:16600635<ref>PMID:16600635</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Human]]

[[Category: Pyridoxal kinase]]

[[Category: Cao, P]]

[[Category: Gong, Y]]

[[Category: Jiang, T]]

[[Category: Tang, L]]

[[Category: Transferase]]