Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family

Research output: Contribution to journalJournal articlepeer-review

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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 journalJournal articlepeer-review

Harvard

Kristensen, O, Laurberg, M, Liljas, A, Kastrup, JSJ & Gajhede, M 2004, 'Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family', Biochemistry, vol. 43, no. 28, pp. 8894-900. https://doi.org/10.1021/bi049083c

APA

Kristensen, O., Laurberg, M., Liljas, A., Kastrup, J. S. J., & Gajhede, M. (2004). Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family. Biochemistry, 43(28), 8894-900. https://doi.org/10.1021/bi049083c

Vancouver

Kristensen O, Laurberg M, Liljas A, Kastrup JSJ, Gajhede M. Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family. Biochemistry. 2004;43(28):8894-900. https://doi.org/10.1021/bi049083c

Author

Kristensen, Ole ; Laurberg, Martin ; Liljas, Anders ; Kastrup, Jette Sandholm Jensen ; Gajhede, Michael. / Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family. In: Biochemistry. 2004 ; Vol. 43, No. 28. pp. 8894-900.

Bibtex

@article{81024f4a8a504dedbb726304d8ca7442,
title = "Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family",
abstract = "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.",
keywords = "Acid Anhydride Hydrolases, Adaptation, Physiological, Bacteria, Bacterial Proteins, Binding Sites, Calcium, Chlorine, Crystallization, Crystallography, X-Ray, Models, Molecular, Molecular Structure, Pyrophosphatases",
author = "Ole Kristensen and Martin Laurberg and Anders Liljas and Kastrup, {Jette Sandholm Jensen} and Michael Gajhede",
year = "2004",
doi = "10.1021/bi049083c",
language = "English",
volume = "43",
pages = "8894--900",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "28",

}

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