PMID- 23104439
OWN - NLM
STAT- MEDLINE
DCOM- 20130712
LR  - 20240204
IS  - 0219-1032 (Electronic)
IS  - 1016-8478 (Print)
IS  - 1016-8478 (Linking)
VI  - 34
IP  - 4
DP  - 2012 Oct
TI  - Crystal structure of pyridoxal biosynthesis lyase PdxS from Pyrococcus 
      horikoshii.
PG  - 407-12
LID - 10.1007/s10059-012-0198-8 [doi]
AB  - Pyridoxal 5'-phosphate (PLP) is the biologically active form of vitamin B(6) and 
      is de novo synthesized from three substrates, dihydroxyacetone phosphate (DHAP), 
      riburose 5-phosphate (RBP), and ammonia hydrolysed from glutamine. Glutamine 
      amidotransferase (PdxT) catalyzes the production of ammonia from glutamine, while 
      PdxS catalyzes the following condensation of ribulose 5-phosphate (Ru5P), 
      glyceraldehyde-3-phosphate (G3P), and ammonia. PdxS exists as a hexamer or 
      dodecamer depending on species and makes a 1:1 complex with PdxT. Pyrococcus 
      horikoshii PdxS has a 37 amino acids insertion region, which is found in some 
      archaeal PdxS proteins, but its structure and function are unknown. To provide 
      further structural information on the role of the insertion region, the 
      oligomeric state, and ligand binding mode of P. horikoshii PdxS, the crystal 
      structure of PdxS from P. horikoshii was solved in two forms: (i) apo form, (ii) 
      r ibose 5-phosphate (R5P) complex and the quaternary structure of PdxS in 
      solution was determined by analytical gel filtration. P. horikoshii PdxS forms 
      hexamer in solution based on analytical gel filtration data. When we superimpose 
      the structure of P. horikoshii PdxS with other dodecamer structures of PdxS, the 
      additional insertion is located apart from the active site and induces a steric 
      clash on the hexamer-hexamer interface of PdxS proteins. Our results suggest that 
      the additional insertion perturbs dodecamer formation of P. horikoshii PdxS.
FAU - Matsuura, Atsushi
AU  - Matsuura A
AD  - Department of Bio & Nano Chemistry, Kookmin University, Seoul 136-702, Korea.
FAU - Yoon, Ji Young
AU  - Yoon JY
FAU - Yoon, Hye-Jin
AU  - Yoon HJ
FAU - Lee, Hyung Ho
AU  - Lee HH
FAU - Suh, Se Won
AU  - Suh SW
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20121018
PL  - United States
TA  - Mol Cells
JT  - Molecules and cells
JID - 9610936
RN  - 0 (Ribulosephosphates)
RN  - 0 (Solutions)
RN  - 3THM379K8A (Pyridoxal)
RN  - 4151-19-3 (ribulose 5-phosphate)
RN  - EC 4.- (Lyases)
SB  - IM
MH  - Amino Acid Sequence
MH  - Crystallography, X-Ray
MH  - Hydrogen Bonding
MH  - Lyases/*chemistry/metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Structure, Quaternary
MH  - Protein Structure, Secondary
MH  - Pyridoxal/*biosynthesis
MH  - Pyrococcus horikoshii/*enzymology
MH  - Ribulosephosphates/metabolism
MH  - Sequence Alignment
MH  - Solutions
PMC - PMC3887772
EDAT- 2012/10/30 06:00
MHDA- 2013/07/16 06:00
PMCR- 2013/10/31
CRDT- 2012/10/30 06:00
PHST- 2012/08/02 00:00 [received]
PHST- 2012/09/06 00:00 [accepted]
PHST- 2012/09/04 00:00 [revised]
PHST- 2012/10/30 06:00 [entrez]
PHST- 2012/10/30 06:00 [pubmed]
PHST- 2013/07/16 06:00 [medline]
PHST- 2013/10/31 00:00 [pmc-release]
AID - S1016-8478(23)07048-6 [pii]
AID - molcell-34-4-407-10 [pii]
AID - 10.1007/s10059-012-0198-8 [doi]
PST - ppublish
SO  - Mol Cells. 2012 Oct;34(4):407-12. doi: 10.1007/s10059-012-0198-8. Epub 2012 Oct 
      18.