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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
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
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
2007-07-09 15:35:24
date last changed
2017-07-30 03:31:12
@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},
  series       = {Biochemistry},
  title        = {Structural characterization of the stringent response related exopolyphosphatase/guanosine pentaphosphate phosphohydrolase protein family},
  url          = {http://dx.doi.org/10.1021/bi049083c},
  volume       = {43},
  year         = {2004},
}