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

Kristensen, O ; Laurberg, Martin LU ; Liljas, Anders LU ; Kastrup, J S and Gajhede, M (2004) In Biochemistry 43(28). p.8894-8900
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 11) at resolutions of 1.53 and 2.15 Angstrom, respectively. This revealed a structural flexibility that has previously been described as a "butterfly-like" cleft opening around the active site in... (More)
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 11) at resolutions of 1.53 and 2.15 Angstrom, 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. (Less)
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author
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Biochemistry
volume
43
issue
28
pages
8894 - 8900
publisher
The American Chemical Society (ACS)
external identifiers
  • wos:000222668000002
  • pmid:15248747
  • scopus:3142666890
ISSN
0006-2960
DOI
10.1021/bi049083c
language
English
LU publication?
yes
id
83aeb631-fb9e-4b20-8945-26cea5e3b5d2 (old id 139386)
date added to LUP
2016-04-01 11:36:16
date last changed
2025-10-14 09:53:42
@article{83aeb631-fb9e-4b20-8945-26cea5e3b5d2,
  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 11) at resolutions of 1.53 and 2.15 Angstrom, 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.}},
  author       = {{Kristensen, O and Laurberg, Martin and Liljas, Anders and Kastrup, J S and Gajhede, M}},
  issn         = {{0006-2960}},
  language     = {{eng}},
  number       = {{28}},
  pages        = {{8894--8900}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Biochemistry}},
  title        = {{Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family}},
  url          = {{http://dx.doi.org/10.1021/bi049083c}},
  doi          = {{10.1021/bi049083c}},
  volume       = {{43}},
  year         = {{2004}},
}