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

Access
View full-text via PolyU eLinks SFX Query
Show full item record

SCOPUSTM   
Citations

10
Last Week
0
Last month
0
Citations as of Sep 19, 2017

WEB OF SCIENCETM
Citations

11
Last Week
0
Last month
0
Citations as of Sep 21, 2017

Page view(s)

47
Last Week
1
Last month
Checked on Sep 17, 2017

Google ScholarTM

Check

Altmetric



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