Please use this identifier to cite or link to this item:
http://hdl.handle.net/10397/27056
Title: | Crystal structure of human pyridoxal kinase | Authors: | Cao, P Gong, Y Tang, L Leung, YC Jiang, T |
Keywords: | Crystal structure Human pyridoxal kinase Perfect twinning Pyridoxal-5′-phosphate |
Issue Date: | 2006 | Source: | Journal of structural biology, 2006, v. 154, no. 3, p. 327-332 How to cite? | Journal: | Journal of Structural Biology | Abstract: | 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 Å 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 β-strand/loop/β-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. | URI: | http://hdl.handle.net/10397/27056 | ISSN: | 1047-8477 | DOI: | 10.1016/j.jsb.2006.02.008 |
Appears in Collections: | Journal/Magazine Article |
Show full item record
SCOPUSTM
Citations
11
Last Week
0
0
Last month
0
0
Citations as of Apr 19, 2018
WEB OF SCIENCETM
Citations
12
Last Week
1
1
Last month
0
0
Citations as of Apr 25, 2018
Page view(s)
57
Last Week
1
1
Last month
Citations as of Apr 23, 2018

Google ScholarTM
Check
Altmetric
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.