4km3
Discovery of a novel structural motif in methionine aminopeptidase from Streptococci with possible post-translational modificationDiscovery of a novel structural motif in methionine aminopeptidase from Streptococci with possible post-translational modification
FunctionFunction
[B2IQ22_STRPS] Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed (By similarity).[HAMAP-Rule:MF_01974]
About this StructureAbout this Structure
4km3 is a 2 chain structure. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Arya T, Kishor C, Saddanapu V, Reddi R, Addlagatta A. Discovery of a new genetic variant of methionine aminopeptidase from Streptococci with possible post-translational modifications: biochemical and structural characterization. PLoS One. 2013 Oct 4;8(10):e75207. doi: 10.1371/journal.pone.0075207. PMID:24124477 doi:http://dx.doi.org/10.1371/journal.pone.0075207