Crystal structure and functional insight of HP0420-homolog from Helicobacter felis.

Crystal structure and functional insight of HP0420-homolog from Helicobacter felis.
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DOI:
10.1016/j.bbrc.2010.03.087
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发表时间:
2010-04-16
影响因子:
3.1
通讯作者:
Ha, Nam-Chul
Ha, Nam-Chul
中科院分区:
生物学4区
文献类型:
--
作者:
Piao, Shunfu;Jin, Xiao Ling;Yun, Bo-Young;Kim, Nahee;Cho, Hyun-Soo;Fukuda, Minoru;Lee, Heeseob;Ha, Nam-Chul

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幽门螺杆菌感染了世界上一半以上的人口,被认为是消化性溃疡疾病和胃癌的原因之一。最近,在幽门螺杆菌中发现了一个假定基因HP0421,它是一种胆固醇α-葡萄糖基转移酶,是合成胆固醇糖苷的酶,而胆固醇糖苷是幽门螺杆菌的重要细胞壁成分。在同一基因簇中,HP0420被共同鉴定,其功能尚不清楚。为了深入了解HP0420的功能,我们报道了HP0420-HP0420同系物的晶体结构。结合尺寸排斥层析的晶体结构表明,HF0420为均二聚体热狗折叠。晶体结构表明,HF0420具有与中心α-螺旋末端保守的组氨酸残基有关的酶活性。随后的生化研究为HP0420和HF0420的功能提供了线索。
Helicobacter pylori infect more than half of the world’s population and are considered a cause of peptic ulcer disease and gastric cancer. Recently, hypothetical gene HP0421 was identified in H. pylori as a cholesterol α-glucosyltransferase, which is required to synthesize cholesteryl glucosides, essential cell wall components of the bacteria. In the same gene-cluster, HP0420 was co-identified, whose function remains unknown. Here we report the crystal structure of HP0420-homolog of H. felis (HF0420) to gain insight into the function of HP0420. The crystal structure, combined with size-exclusion chromatography, reveals that HF0420 adopts a homodimeric hot-dog fold. The crystal structure suggests that HF0420 has enzymatic activity that involves a conserved histidine residue at the end of the central α-helix. Subsequent biochemical studies provide clues to the function of HP0420 and HF0420.
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