1VLP

Crystal structure of a putative nicotinate phosphoribosyltransferase (yor209c, npt1) from saccharomyces cerevisiae at 1.75 A resolution

Summary for 1VLP

• Entry DOI: 10.2210/pdb1vlp/pdb
• Descriptor: nicotinate phosphoribosyltransferase, PHOSPHATE ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: structural genomics, joint center for structural genomics, jcsg, protein structure initiative, psi, transferase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm : P39683
• Total number of polymer chains: 4
• Total formula weight: 204919.78

Authors

Joint Center for Structural Genomics (JCSG) (deposition date: 2004-08-06, release date: 2004-08-24, Last modification date: 2024-11-13)

Primary citation

Chappie, J.S.,Canaves, J.M.,Han, G.W.,Rife, C.L.,Xu, Q.,Stevens, R.C.
The structure of a eukaryotic nicotinic acid phosphoribosyltransferase reveals structural heterogeneity among type II PRTases.
Structure, 13:1385-1396, 2005

PubMed Abstract: Nicotinamide adenine dinucleotide (NAD) is an essential cofactor for cellular redox reactions and can act as an important substrate in numerous biological processes. As a result, nature has evolved multiple biosynthetic pathways to meet this high chemical demand. In Saccharomyces cerevisiae, the NAD salvage pathway relies on the activity of nicotinic acid phosphoribosyltransferase (NAPRTase), a member of the phosphoribosyltransferase (PRTase) superfamily. Here, we report the structure of a eukaryotic (yeast) NAPRTase at 1.75 A resolution (locus name: YOR209C, gene name: NPT1). The structure reveals a two-domain fold that resembles the architecture of quinolinic acid phosphoribosyltransferases (QAPRTases), but with completely different dispositions that provide evidence for structural heterogeneity among the Type II PRTases. The identification of a third domain in NAPRTases provides a structural basis and possible mechanism for the functional modulation of this family of enzymes by ATP.

PubMed: 16154095
DOI: 10.1016/j.str.2005.05.016

Experimental method

X-RAY DIFFRACTION (1.75 Å)