3pn5
From Proteopedia
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{{STRUCTURE_3pn5| PDB=3pn5 | SCENE= }} | {{STRUCTURE_3pn5| PDB=3pn5 | SCENE= }} | ||
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===Crystal structure of Arabidopsis thaliana petide deformylase 1B (AtPDF1B) G41Q mutant=== | ===Crystal structure of Arabidopsis thaliana petide deformylase 1B (AtPDF1B) G41Q mutant=== | ||
+ | {{ABSTRACT_PUBMED_21629676}} | ||
- | + | ==Function== | |
- | + | [[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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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:021629676</ref><references group="xtra"/> | + | <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 07:52, 16 May 2013
Contents |
Crystal structure of Arabidopsis thaliana petide deformylase 1B (AtPDF1B) G41Q mutant
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
3pn5 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
- ↑ 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