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'''E.coli NAD Synthetase, DND''' | '''E.coli NAD Synthetase, DND''' | ||
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Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements., Jauch R, Humm A, Huber R, Wahl MC, J Biol Chem. 2005 Apr 15;280(15):15131-40. Epub 2005 Feb 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15699042 15699042] | Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements., Jauch R, Humm A, Huber R, Wahl MC, J Biol Chem. 2005 Apr 15;280(15):15131-40. Epub 2005 Feb 7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15699042 15699042] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Huber, R.]] | [[Category: Huber, R.]] | ||
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[[Category: Jauch, R.]] | [[Category: Jauch, R.]] | ||
[[Category: Wahl, M C.]] | [[Category: Wahl, M C.]] | ||
[[Category: | [[Category: E coli]] | ||
[[Category: | [[Category: Nad]] | ||
[[Category: | [[Category: Nade]] | ||
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Revision as of 14:16, 3 May 2008
E.coli NAD Synthetase, DND
OverviewOverview
Nicotinamide adenine dinucleotide synthetases (NADS) catalyze the amidation of nicotinic acid adenine dinucleotide (NAAD) to yield the enzyme cofactor nicotinamide adenine dinucleotide (NAD). Here we describe the crystal structures of the ammonia-dependent homodimeric NADS from Escherichia coli alone and in complex with natural substrates and with the reaction product NAD. The structures disclosed two NAAD/NAD binding sites at the dimer interface and an adenosine triphosphate (ATP) binding site within each subunit. Comparison with the Bacillus subtilis NADS showed pronounced chemical differences in the NAAD/NAD binding sites and less prominent differences in the ATP binding pockets. In addition, the E. coli NADS structures revealed unexpected dynamical rearrangements in the NAAD/NAD binding pocket upon NAAD-to-NAD conversion, which define a catalysis state and a substrate/product exchange state. The two states are adopted by concerted movement of the nicotinysyl moieties of NAAD and NAD, Phe-170, and residues 224-228, which may be triggered by differential coordination of a magnesium ion to NAAD and NAD. Phylogenetic structure comparisons suggest that the present results are relevant for designing species-specific antibiotics.
About this StructureAbout this Structure
1WXG is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structures of Escherichia coli NAD synthetase with substrates and products reveal mechanistic rearrangements., Jauch R, Humm A, Huber R, Wahl MC, J Biol Chem. 2005 Apr 15;280(15):15131-40. Epub 2005 Feb 7. PMID:15699042 Page seeded by OCA on Sat May 3 14:16:07 2008