2GG2

Novel bacterial methionine aminopeptidase inhibitors

Summary for 2GG2

• Entry DOI: 10.2210/pdb2gg2/pdb
• Related: 2GG0 2GG3 2GG5 2GG7 2GG8 2GG9 2GGB 2GGC
• Descriptor: Methionine aminopeptidase, COBALT (II) ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: methionine amino peptidase, pita-bread fold, map inhibitor, antibacterial, hydrolase
• Biological source: Escherichia coli K12
• Total number of polymer chains: 1
• Total formula weight: 29648.70

Authors

Evdokimov, A.G.,Pokross, M.E.,Walter, R.L.,Mekel, M. (deposition date: 2006-03-23, release date: 2006-06-13, Last modification date: 2023-08-30)

Primary citation

Evdokimov, A.G.,Pokross, M.,Walter, R.L.,Mekel, M.,Barnett, B.L.,Amburgey, J.,Seibel, W.L.,Soper, S.J.,Djung, J.F.,Fairweather, N.,Diven, C.,Rastogi, V.,Grinius, L.,Klanke, C.,Siehnel, R.,Twinem, T.,Andrews, R.,Curnow, A.
Serendipitous discovery of novel bacterial methionine aminopeptidase inhibitors.
Proteins, 66:538-546, 2007

PubMed Abstract: 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.

PubMed: 17120228
DOI: 10.1002/prot.21207

Experimental method

X-RAY DIFFRACTION (1 Å)