Document Detail


Structure of nicotinic acid mononucleotide adenylyltransferase from Bacillus anthracis.
MedLine Citation:
PMID:  18931430     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Nicotinic acid mononucleotide adenylyltransferase (NaMNAT; EC 2.7.7.18) is the penultimate enzyme in the biosynthesis of NAD(+) and catalyzes the adenylation of nicotinic acid mononucleotide (NaMN) by ATP to form nicotinic acid adenine dinucleotide (NaAD). This enzyme is regarded as a suitable candidate for antibacterial drug development; as such, Bacillus anthracis NaMNAT (BA NaMNAT) was heterologously expressed in Escherichia coli for the purpose of inhibitor discovery and crystallography. The crystal structure of BA NaMNAT was determined by molecular replacement, revealing two dimers per asymmetric unit, and was refined to an R factor and R(free) of 0.228 and 0.263, respectively, at 2.3 A resolution. The structure is very similar to that of B. subtilis NaMNAT (BS NaMNAT), which is also a dimer, and another independently solved structure of BA NaMNAT recently released from the PDB along with two ligated forms. Comparison of these and other less related bacterial NaMNAT structures support the presence of considerable conformational heterogeneity and flexibility in three loops surrounding the substrate-binding area.
Authors:
Shanyun Lu; Craig D Smith; Zhengrong Yang; Pamela S Pruett; Lisa Nagy; Deborah McCombs; Lawrence J Delucas; Wayne J Brouillette; Christie G Brouillette
Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2008-09-30
Journal Detail:
Title:  Acta crystallographica. Section F, Structural biology and crystallization communications     Volume:  64     ISSN:  1744-3091     ISO Abbreviation:  Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.     Publication Date:  2008 Oct 
Date Detail:
Created Date:  2008-10-20     Completed Date:  2008-12-05     Revised Date:  2010-09-21    
Medline Journal Info:
Nlm Unique ID:  101226117     Medline TA:  Acta Crystallogr Sect F Struct Biol Cryst Commun     Country:  England    
Other Details:
Languages:  eng     Pagination:  893-8     Citation Subset:  IM    
Affiliation:
Center for Biophysical Sciences and Engineering, University of Alabama at Birmingham, Birmingham, Alabama 35294-4400, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacillus anthracis / enzymology*,  genetics
Bacterial Proteins / chemistry,  metabolism
Conserved Sequence
Models, Molecular
Molecular Sequence Data
NAD / biosynthesis
Nicotinamide-Nucleotide Adenylyltransferase / chemistry*,  genetics,  metabolism
Protein Conformation
Sequence Alignment
Grant Support
ID/Acronym/Agency:
U01 AI 070386/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 53-84-9/NAD; EC 2.7.7.1/Nicotinamide-Nucleotide Adenylyltransferase; EC 2.7.7.18/nicotinic acid mononucleotide adenylyltransferase
Comments/Corrections

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