| Literature DB >> 18997334 |
Phuong-Thuy Ho Ngo1, Jin-Kwang Kim, Hyesoon Kim, Junho Jung, Yeh-Jin Ahn, Jeong-Gu Kim, Byoung-Moo Lee, Lin-Woo Kang.
Abstract
Peptide deformylase (PDF) catalyzes the removal of the N-formyl group from the N-terminus of newly synthesized polypeptides; this process is crucial for cell survival. As it is an antibacterial drug target against Xanthomonas oryzae pv. oryzae (Xoo), PDF from Xoo was cloned, expressed, purified and crystallized. Native PDF crystals diffracted to 2.7 A resolution and belonged to the hexagonal space group P6(1)22, with unit-cell parameters a = b = 59.0, c = 266.3 A. One monomer is present in the asymmetric unit, with a corresponding crystal volume per protein weight of 3.50 A(3) Da(-1) and a solvent content of 64.9%.Entities:
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Year: 2008 PMID: 18997334 PMCID: PMC2581682 DOI: 10.1107/S1744309108031631
Source DB: PubMed Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun ISSN: 1744-3091