1kaq

Structure of Bacillus subtilis Nicotinic Acid Mononucleotide Adenylyl TransferaseStructure of Bacillus subtilis Nicotinic Acid Mononucleotide Adenylyl Transferase

Structural highlights 1kaq is a 6 chain structure with sequence from "bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: Related: 1kam Gene: nadD ("Bacillus globigii" Migula 1900) Activity: Nicotinate-nucleotide adenylyltransferase, with EC number 2.7.7.18 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [NADD_BACSU] Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The nadD gene, encoding the enzyme nicotinic acid mononucleotide (NaMN) adenylyltransferase (AT), is essential for the synthesis of NAD and subsequent viability of the cell. The nadD gene in Bacillus subtilis (yqeJ) was identified by sequence homology with other bacterial nadD genes and by biochemical characterization of the gene product. NaMN AT catalyzes the reversible adenylation of both NaMN and the nicotinamide mononucleotide (NMN) but shows specificity for the nicotinate. In contrast to other known NMN ATs, biophysical characterizations reveal it to be a dimer. The NaMN AT crystal structure was determined for both the apo enzyme and product-bound form, to 2.1 and 3.2 A, respectively. The structures reveal a "functional" dimer conserved in both crystal forms and a monomer fold common to members of the nucleotidyl-transferase alpha/beta phosphodiesterase superfamily. A structural comparison with family members suggests a new conserved motif (SXXXX(R/K)) at the N terminus of an alpha-helix, which is not part of the shared fold. Interactions of the nicotinic acid with backbone atoms indicate the structural basis for specificity. Identification, characterization, and crystal structure of Bacillus subtilis nicotinic acid mononucleotide adenylyltransferase.,Olland AM, Underwood KW, Czerwinski RM, Lo MC, Aulabaugh A, Bard J, Stahl ML, Somers WS, Sullivan FX, Chopra R J Biol Chem. 2002 Feb 1;277(5):3698-707. Epub 2001 Nov 9. PMID:11704676 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 1kaq, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image