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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Sep 1;65(Pt 9):952-5. doi: 10.1107/S1744309109031467. Epub 2009 Aug 26.
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引用本文的文献

1
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2
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J Biol Chem. 2012 May 25;287(22):18408-17. doi: 10.1074/jbc.M111.309500. Epub 2012 Apr 5.

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来自水稻白叶枯病菌(Xanthomonas oryzae pv. oryzae)pepA基因的亮氨酸氨肽酶(LAP)的克隆、表达、结晶及初步X射线晶体学分析

Cloning, expression, crystallization and preliminary X-ray crystallographic analysis of leucine aminopeptidase (LAP) from the pepA gene of Xanthomonas oryzae pv. oryzae.

作者信息

Huynh Kim-Hung, Natarajan Sampath, Choi Jeongyoon, Song Na-Hyun, Kim Jeong-Gu, Lee Byoung-Moo, Ahn Yeh-Jin, Kang Lin-Woo

机构信息

Department of Advanced Technology Fusion, Konkuk University, Seoul, Republic of Korea.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Sep 1;65(Pt 9):952-5. doi: 10.1107/S1744309109031467. Epub 2009 Aug 26.

DOI:10.1107/S1744309109031467
PMID:19724142
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2795610/
Abstract

Xanthomonas oryzae pv. oryzae (Xoo) causes the serious disease bacterial blight in rice. The pepA (Xoo0834) gene from Xoo is one of around 100 genes that have been selected for the design of antibacterial drugs. The pepA gene encodes leucine aminopeptidase (LAP), an exopeptidase that catalyzes the hydrolysis of leucine residues from the N-terminus of a protein or peptide. This enzyme was expressed in Escherichia coli, purified and crystallized, and preliminary X-ray structural studies have been carried out. The LAP crystal diffracted to 2.6 A resolution and belonged to the cubic space group P2(1)3. The unit-cell volume of the crystal was compatible with the presence of two monomers in the asymmetric unit.

摘要

水稻白叶枯病菌(Xanthomonas oryzae pv. oryzae,Xoo)可引发水稻的严重病害——白叶枯病。来自Xoo的pepA(Xoo0834)基因是已被选定用于抗菌药物设计的约100个基因之一。pepA基因编码亮氨酸氨肽酶(LAP),这是一种外肽酶,可催化从蛋白质或肽的N端水解亮氨酸残基。该酶在大肠杆菌中表达、纯化并结晶,并已进行了初步的X射线结构研究。LAP晶体的衍射分辨率为2.6 Å,属于立方空间群P2(1)3。该晶体的晶胞体积与不对称单元中存在两个单体相符。