The solution structure of the outer membrane lipoprotein OmlA from Xanthomonas axonopodis pv. citri reveals a protein fold implicated in protein–protein interaction
The solution structure of the outer membrane lipoprotein OmlA from Xanthomonas axonopodis pv. citri reveals a protein fold implicated in protein–protein interaction
复制标题
柑橘黄单胞菌外膜脂蛋白 OmlA 的溶液结构揭示了与蛋白质-蛋白质相互作用有关的蛋白质折叠。
DOI:
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发表时间:
2008
期刊:
影响因子:
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通讯作者:
C. Benedetti
中科院分区:
文献类型:
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作者:
M. M. T. Vanini;A. Spisni;M. Sforça;T. Pertinhez;C. Benedetti
The outer membrane lipoprotein A (OmlA) belongs to a family of bacterial small lipoproteins widely distributed across the beta and gamma proteobacteria. Although the role of numerous bacterial lipoproteins is known, the biological function of OmlA remains elusive. We found that in the citrus canker pathogen, Xanthomonas axonopodis pv. citri (X. citri), OmlA is coregulated with the ferric uptake regulator (Fur) and their expression is enhanced when X. citri is grown on citrus leaves, suggesting that these proteins are involved in plant‐pathogen interaction. To gain insights into the function of OmlA, its conformational and dynamic features were determined by nuclear magnetic resonance. The protein has highly flexible N‐ and C‐ termini and a structurally well defined core composed of three β‐strands and two small α‐helices, which pack against each other forming a two‐layer alpha/beta scaffold. This protein fold resembles the domains of the β‐lactamase inhibitory protein BLIP, involved in protein–protein binding. In conclusion, the structure of OmlA does suggest that this protein may be implicated in protein–protein interactions required during X. citri infection. Proteins 2008. © 2008 Wiley‐Liss, Inc.
影响因子:
2.9
作者:
Lefevre, JF;Dayie, KT;Wagner, G
通讯作者:
Wagner, G
影响因子:
2.9
作者:
Parsons, LM;Lin, F;Orban, J
通讯作者:
Orban, J