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Crystallization and preliminary crystallographic studies of Helicobacter pylori arginase.


ABSTRACT: Helicobacter pylori arginase is an important factor in evasion of the host's immune system and contributes to persistent infection by this bacterium. It is unique in many aspects compared with other arginases: for example, it has optimal activity with Co(2+) as a cofactor rather than Mn(2+) and has strongest activity at acidic pH instead of alkaline pH. In this study, H. pylori arginase was purified and crystallized in complex with Mn(2+) and a diffraction data set was collected to 2.2?Å resolution. The crystals belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 94.69, b = 102.24, c = 148.61?Å.

SUBMITTER: Zhang J 

PROVIDER: S-EPMC3107149 | biostudies-literature | 2011 Jun

REPOSITORIES: biostudies-literature

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Crystallization and preliminary crystallographic studies of Helicobacter pylori arginase.

Zhang Jinyong J   Zhang Xiaoli X   Mao Xuhu X   Zou Quanming Q   Li Defeng D  

Acta crystallographica. Section F, Structural biology and crystallization communications 20110526 Pt 6


Helicobacter pylori arginase is an important factor in evasion of the host's immune system and contributes to persistent infection by this bacterium. It is unique in many aspects compared with other arginases: for example, it has optimal activity with Co(2+) as a cofactor rather than Mn(2+) and has strongest activity at acidic pH instead of alkaline pH. In this study, H. pylori arginase was purified and crystallized in complex with Mn(2+) and a diffraction data set was collected to 2.2 Å resolut  ...[more]

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