Insights into the substrate specificity of plant peptide deformylase, an essential enzyme with potential for the development of novel biotechnology applications in agriculture
In: Biochemical Journal, Jg. 413 (2008-07-15), S. 417-427
Online
unknown
Zugriff:
The crystal structure of AtPDF1B [Arabidopsis thaliana PDF (peptide deformylase) 1B; EC 3.5.1.88], a plant specific deformylase, has been determined at a resolution of 2.4 {angstrom} (1 {angstrom}=0.1 nm). The overall fold of AtPDF1B is similar to other peptide deformylases that have been reported. Evidence from the crystal structure and gel filtration chromatography indicates that AtPDF1B exists as a symmetric dimer. PDF1B is essential in plants and has a preferred substrate specificity towards the PS II (photosystem II) D1 polypeptide. Comparative analysis of AtPDF1B, AtPDF1A, and the type 1B deformylase from Escherichia coli, identifies a number of differences in substrate binding subsites that might account for variations in sequence preference. A model of the N-terminal five amino acids from the D1 polypeptide bound in the active site of AtPDF1B suggests an influence of Tyr{sup 178} as a structural determinant for polypeptide substrate specificity through hydrogen bonding with Thr{sup 2} in the D1 sequence. Kinetic analyses using a polypeptide mimic of the D1 N-terminus was performed on AtPDF1B mutated at Tyr{sup 178} to alanine, phenylalanine or arginine (equivalent residue in AtPDF1A). The results suggest that, whereas Tyr{sup 178} can influence catalytic activity, other residues contribute to the overall preference for themore » D1 polypeptide.« less
Titel: |
Insights into the substrate specificity of plant peptide deformylase, an essential enzyme with potential for the development of novel biotechnology applications in agriculture
|
---|---|
Autor/in / Beteiligte Person: | Schmidt, Jack ; Williams, Mark A. ; Houtz, Robert L. ; Cai, Yiying ; Lynnette M.A. Dirk ; Grossman, Robert B. ; Nayak, Nihar R. ; Rodgers, David W. ; Barnes, Jonathan C. ; Hanger, Katherine M. |
Link: | |
Zeitschrift: | Biochemical Journal, Jg. 413 (2008-07-15), S. 417-427 |
Veröffentlichung: | Portland Press Ltd., 2008 |
Medientyp: | unknown |
ISSN: | 1470-8728 (print) ; 0264-6021 (print) |
DOI: | 10.1042/bj20071641 |
Schlagwort: |
|
Sonstiges: |
|