1lw7
From Proteopedia
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NADR PROTEIN FROM HAEMOPHILUS INFLUENZAE
Overview
Haemophilus influenzae NadR protein (hiNadR) has been shown to be a, bifunctional enzyme possessing both NMN adenylytransferase (NMNAT; EC ), and ribosylnicotinamide kinase (RNK; EC ) activities. Its function is, essential for the growth and survival of H. influenzae and thus may, present a new highly specific anti-infectious drug target. We have solved, the crystal structure of hiNadR complexed with NAD using the, selenomethionine MAD phasing method. The structure reveals the presence of, two distinct domains. The N-terminal domain that hosts the NMNAT activity, is closely related to archaeal NMNAT, whereas the C-terminal domain, which, has been experimentally demonstrated to possess ribosylnicotinamide kinase, activity, is structurally similar to yeast thymidylate kinase and several, other P-loop-containing kinases. There appears to be no cross-talk between, the two active sites. The bound NAD at the active site of the NMNAT domain, reveals several critical interactions between NAD and the protein. There, is also a second non-active-site NAD molecule associated with the, C-terminal RNK domain that adopts a highly folded conformation with the, nicotinamide ring stacking over the adenine base. Whereas the RNK domain, of the hiNadR structure presented here is the first structural, characterization of a ribosylnicotinamide kinase from any organism, the, NMNAT domain of hiNadR defines yet another member of the pyridine, nucleotide adenylyltransferase family.
About this Structure
1LW7 is a Single protein structure of sequence from Haemophilus influenzae with SO4 and NAD as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of Haemophilus influenzae NadR protein. A bifunctional enzyme endowed with NMN adenyltransferase and ribosylnicotinimide kinase activities., Singh SK, Kurnasov OV, Chen B, Robinson H, Grishin NV, Osterman AL, Zhang H, J Biol Chem. 2002 Sep 6;277(36):33291-9. Epub 2002 Jun 14. PMID:12068016
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