This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


4km3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
'''Unreleased structure'''
+
{{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 entry 4km3 is ON HOLD until Paper Publication
+
==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]
-
Authors: Arya, T., Addlagatta, A.
+
==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].
-
Description: Discovery of a novel structural motif in methionine aminopeptidase from Streptococci with possible post-translational modification
+
==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

Template:STRUCTURE 4km3

Contents

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:http://dx.doi.org/10.1371/journal.pone.0075207

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4km3"
Personal tools