1F9A

CRYSTAL STRUCTURE ANALYSIS OF NMN ADENYLYLTRANSFERASE FROM METHANOCOCCUS JANNASCHII

Summary for 1F9A

• Entry DOI: 10.2210/pdb1f9a/pdb
• Descriptor: HYPOTHETICAL PROTEIN MJ0541, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: alpha/beta, transferase, hypothetical protein, structural genomics
• Biological source: Methanocaldococcus jannaschii
• Total number of polymer chains: 6
• Total formula weight: 120919.10

Authors

D'Angelo, I.,Raffaelli, N.,Dabusti, V.,Lorenzi, T.,Magni, G.,Rizzi, M. (deposition date: 2000-07-09, release date: 2001-01-10, Last modification date: 2024-02-07)

Primary citation

D'Angelo, I.,Raffaelli, N.,Dabusti, V.,Lorenzi, T.,Magni, G.,Rizzi, M.
Structure of nicotinamide mononucleotide adenylyltransferase: a key enzyme in NAD(+) biosynthesis.
Structure Fold.Des., 8:993-1004, 2000

PubMed Abstract: Nicotinamide adenine dinucleotide (NAD(+)) is an essential cofactor involved in fundamental processes in cell metabolism. The enzyme nicotinamide mononucleotide adenylyltransferase (NMN AT) plays a key role in NAD(+) biosynthesis, catalysing the condensation of nicotinamide mononucleotide and ATP, and yielding NAD(+) and pyrophosphate. Given its vital role in cell life, the enzyme represents a possible target for the development of new antibacterial agents.

PubMed: 10986466
DOI: 10.1016/S0969-2126(00)00190-8

Experimental method

X-RAY DIFFRACTION (2 Å)