5gp0

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Crystal structure of geraniol-NUDX1 complexCrystal structure of geraniol-NUDX1 complex

Structural highlights

5gp0 is a 4 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.702Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

NUDT1_ARATH Mediates the hydrolysis of some nucleoside diphosphate derivatives. Its substrate specificity is unclear. In vitro, it can use NTP, dNTP, 8-oxo-GTP, 8-oxo-dGTP, dGTP, dATP, dTTP or dihydroneopterin triphosphate (DHNTP) as substrate. Has some NADH pyrophosphatase activity in vitro; however, such activity may not be relevant in vivo due to the high concentration of manganese used during the experiments. Plays an important role in protection against oxidative DNA and RNA damage by removing oxidatively damaged form of guanine.[1] [2] [3]

See Also

References

  1. Klaus SM, Wegkamp A, Sybesma W, Hugenholtz J, Gregory JF 3rd, Hanson AD. A nudix enzyme removes pyrophosphate from dihydroneopterin triphosphate in the folate synthesis pathway of bacteria and plants. J Biol Chem. 2005 Feb 18;280(7):5274-80. Epub 2004 Dec 16. PMID:15611104 doi:http://dx.doi.org/M413759200
  2. Ogawa T, Ueda Y, Yoshimura K, Shigeoka S. Comprehensive analysis of cytosolic Nudix hydrolases in Arabidopsis thaliana. J Biol Chem. 2005 Jul 1;280(26):25277-83. Epub 2005 May 5. PMID:15878881 doi:http://dx.doi.org/M503536200
  3. Yoshimura K, Ogawa T, Ueda Y, Shigeoka S. AtNUDX1, an 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-triphosphate pyrophosphohydrolase, is responsible for eliminating oxidized nucleotides in Arabidopsis. Plant Cell Physiol. 2007 Oct;48(10):1438-49. Epub 2007 Sep 5. PMID:17804481 doi:http://dx.doi.org/10.1093/pcp/pcm112

5gp0, resolution 1.70Å

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OCA