4km3: Difference between revisions
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{{STRUCTURE_4km3| PDB=4km3 | SCENE= }} | |||
===Discovery of a novel structural motif in methionine aminopeptidase from Streptococci with possible post-translational modification=== | |||
{{ABSTRACT_PUBMED_24124477}} | |||
The | ==Function== | ||
[[http://www.uniprot.org/uniprot/B2IQ22_STRPS 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 Structure== | |||
[[4km3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KM3 OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:024124477</ref><references group="xtra"/><references/> | |||
[[Category: Addlagatta, A.]] | |||
[[Category: Arya, T.]] | |||
[[Category: Classification]] | |||
[[Category: Hydrolase]] | |||
Revision as of 08:17, 15 January 2014
Discovery of a novel structural motif in methionine aminopeptidase from Streptococci with possible post-translational modification
Template:ABSTRACT PUBMED 24124477
Function
[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 Structure
4km3 is a 2 chain structure. Full crystallographic information is available from OCA.
Reference
- 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:https://dx.doi.org/10.1371/journal.pone.0075207
