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3pn4

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[[Image:3pn4.png|left|200px]]
 
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{{STRUCTURE_3pn4| PDB=3pn4 | SCENE= }}
{{STRUCTURE_3pn4| PDB=3pn4 | SCENE= }}
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===Crystal structure of Arabidopsis thaliana petide deformylase 1B (AtPDF1B) in complex with actinonin (crystallized in PEG-550-MME)===
===Crystal structure of Arabidopsis thaliana petide deformylase 1B (AtPDF1B) in complex with actinonin (crystallized in PEG-550-MME)===
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{{ABSTRACT_PUBMED_21629676}}
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==Function==
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[[http://www.uniprot.org/uniprot/DEF1B_ARATH DEF1B_ARATH]] Removes the formyl group from the N-terminal Met of newly synthesized proteins. Has a preferred substrate specificity towards the photosystem II (PS II) D1 polypeptide.<ref>PMID:11060042</ref>
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{{ABSTRACT_PUBMED_21629676}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:021629676</ref><references group="xtra"/>
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<ref group="xtra">PMID:021629676</ref><references group="xtra"/><references/>
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Peptide deformylase]]
[[Category: Peptide deformylase]]

Revision as of 07:45, 16 May 2013

Template:STRUCTURE 3pn4

Contents

Crystal structure of Arabidopsis thaliana petide deformylase 1B (AtPDF1B) in complex with actinonin (crystallized in PEG-550-MME)

Template:ABSTRACT PUBMED 21629676

Function

[DEF1B_ARATH] Removes the formyl group from the N-terminal Met of newly synthesized proteins. Has a preferred substrate specificity towards the photosystem II (PS II) D1 polypeptide.[1]

About this Structure

3pn4 is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

  • Fieulaine S, Boularot A, Artaud I, Desmadril M, Dardel F, Meinnel T, Giglione C. Trapping conformational States along ligand-binding dynamics of Peptide deformylase: the impact of induced fit on enzyme catalysis. PLoS Biol. 2011 May;9(5):e1001066. Epub 2011 May 24. PMID:21629676 doi:10.1371/journal.pbio.1001066
  1. ↑ Giglione C, Serero A, Pierre M, Boisson B, Meinnel T. Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms. EMBO J. 2000 Nov 1;19(21):5916-29. PMID:11060042 doi:10.1093/emboj/19.21.5916

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OCA

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