1B9L

7,8-DIHYDRONEOPTERIN TRIPHOSPHATE EPIMERASE

Summary for 1B9L

• Entry DOI: 10.2210/pdb1b9l/pdb
• Descriptor: PROTEIN (EPIMERASE) (1 entity in total)
• Functional Keywords: epimerase, isomerase
• Biological source: Escherichia coli
• Total number of polymer chains: 8
• Total formula weight: 112824.19

Authors

Ploom, T.,Haussmann, C.,Hof, P.,Steinbacher, S.,Bacher, A.,Richardson, J.,Huber, R. (deposition date: 1999-02-11, release date: 2000-02-18, Last modification date: 2023-12-27)

Primary citation

Ploom, T.,Haussmann, C.,Hof, P.,Steinbacher, S.,Bacher, A.,Richardson, J.,Huber, R.
Crystal structure of 7,8-dihydroneopterin triphosphate epimerase.
Structure Fold.Des., 7:509-516, 1999

PubMed Abstract: Dihydroneopterin triphosphate (H2NTP) is the central substrate in the biosynthesis of folate and tetrahydrobiopterin. Folate serves as a cofactor in amino acid and purine biosynthesis and tetrahydrobiopterin is used as a cofactor in amino acid hydroxylation and nitric oxide synthesis. In bacteria, H2NTP enters the folate biosynthetic pathway after nonenzymatic dephosphorylation; in vertebrates, H2NTP is used to synthesize tetrahydrobiopterin. The dihydroneopterin triphosphate epimerase of Escherichia coli catalyzes the inversion of carbon 2' of H2NTP.

PubMed: 10378270
DOI: 10.1016/S0969-2126(99)80067-7

Experimental method

X-RAY DIFFRACTION (2.9 Å)