2h2a

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spinqualitylabelsall models 2h2a, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of Nicotinic acid mononucleotide adenylyltransferase from Staphylococcus aureus: product bound form 2

Overview

Bacterial nicotinic acid mononucleotide adenylyltransferase (NaMNAT; EC, 2.7.7.18) encoded by the nadD gene, is essential for cell survival and is, thus an attractive target for developing new antibacterial agents. The, NaMNAT catalyzes the transfer of an adenylyl group of ATP to nicotinic, acid mononucleotide (NaMN) to form nicotinic acid dinucleotide (NaAD). Two, independently derived, high-resolution structures of Staphylococcus aureus, NaMNAT-NaAD complexes establish the conserved features of the core, dinucleotide-binding fold with other adenylyltransferases from bacteria to, human despite a limited sequence conservation. The crystal structures, reveal that the nicotinate carboxylates of NaAD are recognized by, interaction with the main-chain amides of Thr85 and Tyr117, a positive, helix dipole and two bridged-water molecules. Unlike other bacterial, adenylyltransferases, where a partially conserved histidine residue, interacts with the nicotinate ring, the Leu44 side-chain interacts with, the nicotinate ring by van der Waals contact. Importantly, the S. aureus, NaMNAT represents a distinct adenylyltransferase subfamily identifiable in, part by common features of dimerization and substrate recognition in the, loop connecting beta5 to beta6 (residues 132-146) and the additional beta6, strand. The unique beta6 strand helps orient the residues in the loop, connecting beta5 to beta6 for substrate/product recognition and allows the, beta7 strand structural flexibility to make key dimer interface, interactions. Taken together, these structural results provide a molecular, basis for understanding the coupled activity and recognition specificity, for S. aureus NaMNAT and for rational design of selective inhibitors.

About this Structure

2H2A is a Single protein structure of sequence from Staphylococcus aureus with CA, DND and GOL as ligands. Active as Nicotinate-nucleotide adenylyltransferase, with EC number 2.7.7.18 Full crystallographic information is available from OCA.

Reference

Crystal structure of nicotinic acid mononucleotide adenylyltransferase from Staphyloccocus aureus: structural basis for NaAD interaction in functional dimer., Han S, Forman MD, Loulakis P, Rosner MH, Xie Z, Wang H, Danley DE, Yuan W, Schafer J, Xu Z, J Mol Biol. 2006 Jul 21;360(4):814-25. Epub 2006 Jun 6. PMID:16784754

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