1k4m: Difference between revisions

Revision as of 09:44, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1k4m.png

Template:STRUCTURE 1k4m

Crystal structure of E.coli nicotinic acid mononucleotide adenylyltransferase complexed to deamido-NADCrystal structure of E.coli nicotinic acid mononucleotide adenylyltransferase complexed to deamido-NAD

Template:ABSTRACT PUBMED 11796112

About this StructureAbout this Structure

1K4M is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures of E. coli nicotinate mononucleotide adenylyltransferase and its complex with deamido-NAD., Zhang H, Zhou T, Kurnasov O, Cheek S, Grishin NV, Osterman A, Structure. 2002 Jan;10(1):69-79. PMID:11796112

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of E.coli nicotinic acid mononucleotide adenylyltransferase complexed to deamido-NAD'''
+===Crystal structure of E.coli nicotinic acid mononucleotide adenylyltransferase complexed to deamido-NAD===
-==Overview==
+<!--
-Nicotinamide/Nicotinate mononucleotide (NMN/NaMN) adenylyltransferase is an indispensable enzyme in both de novo biosynthesis and salvage of NAD+ and NADP+. In prokaryotes, it is absolutely required for cell survival, thus representing an attractive target for the development of new broad-spectrum antibacteria inhibitors. The crystal structures of E. coli NaMN adenylyltransferase (NMNAT) and its complex with deamido-NAD (NaAD) revealed that ligand binding causes large conformational changes in several loop regions around the active site. The enzyme specifically recognizes the deamidated pyridine nucleotide through interactions between nicotinate carboxylate with several protein main chain amides and a positive helix dipole. Comparison of E. coli NMNAT with those from archaeal organisms revealed extensive differences in the active site architecture, enzyme-ligand interaction mode, and bound dinucleotide conformations. The bacterial NaMN adenylyltransferase structures described here provide a foundation for structure-based design of specific inhibitors that may have therapeutic potential.
+The line below this paragraph, {{ABSTRACT_PUBMED_11796112}}, adds the Publication Abstract to the page
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 [[Category: Zhou, T.]]
 [[Category: Nucleotidyltransferase]]
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