2ggb
Novel bacterial methionine aminopeptidase inhibitors
|
OverviewOverview
In this article we describe the application of structural biology methods, to the discovery of novel potent inhibitors of methionine aminopeptidases., These enzymes are employed by the cells to cleave the N-terminal, methionine from nascent peptides and proteins. As this is one of the, critical steps in protein maturation, it is very likely that inhibitors of, these enzymes may prove useful as novel antibacterial agents. Involvement, of crystallography at the very early stages of the inhibitor design, process resulted in serendipitous discovery of a new inhibitor class, the, pyrazole-diamines. Atomic-resolution structures of several inhibitors, bound to the enzyme illuminate a new mode of inhibitor binding.
About this StructureAbout this Structure
2GGB is a Single protein structure of sequence from Escherichia coli with CO, NA and U17 as ligands. Active as Methionyl aminopeptidase, with EC number 3.4.11.18 Full crystallographic information is available from OCA.
ReferenceReference
Serendipitous discovery of novel bacterial methionine aminopeptidase inhibitors., Evdokimov AG, Pokross M, Walter RL, Mekel M, Barnett BL, Amburgey J, Seibel WL, Soper SJ, Djung JF, Fairweather N, Diven C, Rastogi V, Grinius L, Klanke C, Siehnel R, Twinem T, Andrews R, Curnow A, Proteins. 2007 Feb 15;66(3):538-46. PMID:17120228
Page seeded by OCA on Wed Nov 21 11:11:36 2007