Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family
Research output: Contribution to journal › Journal article › peer-review
Standard
Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family. / Kristensen, Ole; Laurberg, Martin; Liljas, Anders; Kastrup, Jette Sandholm Jensen; Gajhede, Michael.
In: Biochemistry, Vol. 43, No. 28, 2004, p. 8894-900.Research output: Contribution to journal › Journal article › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
RIS
TY - JOUR
T1 - Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family
AU - Kristensen, Ole
AU - Laurberg, Martin
AU - Liljas, Anders
AU - Kastrup, Jette Sandholm Jensen
AU - Gajhede, Michael
PY - 2004
Y1 - 2004
N2 - Exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GPPA) enzymes play central roles in the bacterial stringent response induced by starvation. The high-resolution crystal structure of the putative Aquifex aeolicus PPX/GPPA phosphatase from the actin-like ATPase domain superfamily has been determined, providing the first insights to features of the common catalytic core of the PPX/GPPA family. The protein has a two-domain structure with an active site located in the interdomain cleft. Two crystal forms were investigated (type I and II) at resolutions of 1.53 and 2.15 A, respectively. This revealed a structural flexibility that has previously been described as a "butterfly-like" cleft opening around the active site in other actin-like superfamily proteins. A calcium ion is observed at the center of this region in type I crystals, substantiating that PPX/GPPA enzymes use metal ions for catalysis. Structural analysis suggests that nucleotides bind at a similar position to that seen in other members of the superfamily.
AB - Exopolyphosphatase/guanosine pentaphosphate phosphohydrolase (PPX/GPPA) enzymes play central roles in the bacterial stringent response induced by starvation. The high-resolution crystal structure of the putative Aquifex aeolicus PPX/GPPA phosphatase from the actin-like ATPase domain superfamily has been determined, providing the first insights to features of the common catalytic core of the PPX/GPPA family. The protein has a two-domain structure with an active site located in the interdomain cleft. Two crystal forms were investigated (type I and II) at resolutions of 1.53 and 2.15 A, respectively. This revealed a structural flexibility that has previously been described as a "butterfly-like" cleft opening around the active site in other actin-like superfamily proteins. A calcium ion is observed at the center of this region in type I crystals, substantiating that PPX/GPPA enzymes use metal ions for catalysis. Structural analysis suggests that nucleotides bind at a similar position to that seen in other members of the superfamily.
KW - Acid Anhydride Hydrolases
KW - Adaptation, Physiological
KW - Bacteria
KW - Bacterial Proteins
KW - Binding Sites
KW - Calcium
KW - Chlorine
KW - Crystallization
KW - Crystallography, X-Ray
KW - Models, Molecular
KW - Molecular Structure
KW - Pyrophosphatases
U2 - 10.1021/bi049083c
DO - 10.1021/bi049083c
M3 - Journal article
C2 - 15248747
VL - 43
SP - 8894
EP - 8900
JO - Biochemistry
JF - Biochemistry
SN - 0006-2960
IS - 28
ER -
ID: 40318589