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来自水稻黄单胞菌稻瘟病菌株的肽脱甲酰基酶的表达、结晶及初步X射线晶体学分析

Expression, crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Xanthomonas oryzae pv. oryzae.

作者信息

Ngo Phuong-Thuy Ho, Kim Jin-Kwang, Kim Hyesoon, Jung Junho, Ahn Yeh-Jin, Kim Jeong-Gu, Lee Byoung-Moo, Kang Lin-Woo

机构信息

Department of Advanced Technology Fusion, Konkuk University, Hwayang-dong, Gwangjin-gu, Seoul 143-701, Republic of Korea.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Nov 1;64(Pt 11):1031-3. doi: 10.1107/S1744309108031631. Epub 2008 Oct 28.

DOI:10.1107/S1744309108031631
PMID:18997334
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2581682/
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%.

摘要

肽脱甲酰基酶（PDF）催化从新合成多肽的N末端去除N-甲酰基；该过程对细胞存活至关重要。由于它是针对水稻白叶枯病菌（Xoo）的抗菌药物靶点，因此克隆、表达、纯化并结晶了来自Xoo的PDF。天然PDF晶体的衍射分辨率为2.7 Å，属于六方空间群P6(1)22，晶胞参数a = b = 59.0，c = 266.3 Å。不对称单元中存在一个单体，每个蛋白质重量对应的晶体体积为3.50 Å(3) Da(-1)，溶剂含量为64.9%。

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