4km3

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'''Unreleased structure'''
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{{STRUCTURE_4km3| PDB=4km3 | SCENE= }}
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===Discovery of a novel structural motif in methionine aminopeptidase from Streptococci with possible post-translational modification===
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{{ABSTRACT_PUBMED_24124477}}
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The entry 4km3 is ON HOLD until Paper Publication
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==Function==
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[[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]
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Authors: Arya, T., Addlagatta, A.
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==About this Structure==
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[[4km3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4KM3 OCA].
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Description: Discovery of a novel structural motif in methionine aminopeptidase from Streptococci with possible post-translational modification
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==Reference==
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<ref group="xtra">PMID:024124477</ref><references group="xtra"/><references/>
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[[Category: Addlagatta, A.]]
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[[Category: Arya, T.]]
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[[Category: Classification]]
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[[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

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