1QAP

QUINOLINIC ACID PHOSPHORIBOSYLTRANSFERASE WITH BOUND QUINOLINIC ACID

Summary for 1QAP

• Entry DOI: 10.2210/pdb1qap/pdb
• Descriptor: QUINOLINIC ACID PHOSPHORIBOSYLTRANSFERASE, QUINOLINIC ACID (3 entities in total)
• Functional Keywords: glycosyltransferase, quinolinic acid, nad biosynthesis
• Biological source: Salmonella typhimurium
• Total number of polymer chains: 2
• Total formula weight: 65295.44

Authors

Eads, J.C.,Ozturk, D.,Wexler, T.B.,Grubmeyer, C.,Sacchettini, J.C. (deposition date: 1996-09-20, release date: 1997-03-12, Last modification date: 2024-02-14)

Primary citation

Eads, J.C.,Ozturk, D.,Wexler, T.B.,Grubmeyer, C.,Sacchettini, J.C.
A new function for a common fold: the crystal structure of quinolinic acid phosphoribosyltransferase.
Structure, 5:47-58, 1997

PubMed Abstract: Quinolinic acid (QA) is a neurotoxin and has been shown to be present at high levels in the central nervous system of patients with certain diseases, such as AIDS and meningitis. The enzyme quinolinic acid phosphoribosyltransferase (QAPRTase) provides the only route for QA metabolism and is also an essential step in de novo NAD biosynthesis. QAPRTase catalyzes the synthesis of nicotinic acid mononucleotide (NAMN) from QA and 5-phosphoribosyl-1-pyrophosphate (PRPP). The structures of several phosphoribosyltransferases (PRTases) have been reported, and all have shown a similar fold of a five-strandard beta sheet surrounded by four alpha helices. A conserved sequence motif of 13 residues is common to these 'type I' PRTases but is not observed in the QAPRTase sequence, suggestive of a different fold for this enzyme.

PubMed: 9016724
DOI: 10.1016/S0969-2126(97)00165-2

Experimental method

X-RAY DIFFRACTION (2.8 Å)