PMID- 9548738
OWN - NLM
STAT- MEDLINE
DCOM- 19980514
LR  - 20131121
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 37
IP  - 15
DP  - 1998 Apr 14
TI  - The crystal structure of phosphoribulokinase from Rhodobacter sphaeroides reveals 
      a fold similar to that of adenylate kinase.
PG  - 5074-85
AB  - The essential photosynthetic enzyme phosphoribulokinase (PRK) is responsible for 
      the conversion of ribulose 5-phosphate (Ru5P) to ribulose 1,5-bisphosphate, the 
      substrate for the CO2 fixing enzyme ribulose 1,5-bisphosphate 
      carboxylase/oxygenase (Rubisco). We have determined the structure of the 
      octameric bacterial form of PRK to a resolution of 2.5 A. The protein is folded 
      into a seven-member mixed beta-sheet surrounded by alpha-helices, giving the 
      overall appearance of the nucleotide monophosphate family of kinases. Homology 
      with the nucleotide monophosphate kinases suggests a number of amino acid 
      residues that are likely to be important in catalysis and suggests the roles of 
      some amino acid residues that have been mutated prior to the determination of the 
      structure. Further, sequence identity across eukaryotic and prokaryotic species 
      and a calculation of the buried surface area suggests the identity within the 
      octamer of a dimer conserved throughout evolution. The width of the groove 
      leading to the active site is consistent with an oriented molecule of thioredoxin 
      controlling the oxidation state of two cysteines that regulate activity in the 
      eukaryotic enzymes. Although neither Asp 42 nor Asp 169 can be definitively 
      assigned as the catalytic base, the crystal structure suggests the location of a 
      ribulose 5-phosphate binding site and suggests a role for several of the 
      conserved basic residues.
FAU - Harrison, D H
AU  - Harrison DH
AD  - Department of Biochemistry, Medical College of Wisconsin, Milwaukee, Wisconsin 
      53226, USA.
FAU - Runquist, J A
AU  - Runquist JA
FAU - Holub, A
AU  - Holub A
FAU - Miziorko, H M
AU  - Miziorko HM
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor))
RN  - EC 2.7.1.19 (phosphoribulokinase)
RN  - EC 2.7.4.3 (Adenylate Kinase)
RN  - K848JZ4886 (Cysteine)
SB  - IM
MH  - Adenylate Kinase/chemistry
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Computer Simulation
MH  - Conserved Sequence
MH  - Crystallography, X-Ray
MH  - Cysteine
MH  - Evolution, Molecular
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Oxidation-Reduction
MH  - Phosphotransferases (Alcohol Group Acceptor)/*chemistry
MH  - Protein Conformation
MH  - Protein Folding
MH  - Rhodobacter sphaeroides/*enzymology
MH  - Species Specificity
EDAT- 1998/05/16 00:00
MHDA- 1998/05/16 00:01
CRDT- 1998/05/16 00:00
PHST- 1998/05/16 00:00 [pubmed]
PHST- 1998/05/16 00:01 [medline]
PHST- 1998/05/16 00:00 [entrez]
AID - bi972805y [pii]
AID - 10.1021/bi972805y [doi]
PST - ppublish
SO  - Biochemistry. 1998 Apr 14;37(15):5074-85. doi: 10.1021/bi972805y.