根癌农杆菌新型谷胱甘肽S-转移酶（ATU5508）在2.0埃分辨率下的比较结构分析。

Comparative structural analysis of a novel glutathioneS-transferase (ATU5508) from Agrobacterium tumefaciens at 2.0 A resolution.

作者信息

Kosloff Mickey, Han Gye Won, Krishna S Sri, Schwarzenbacher Robert, Fasnacht Marc, Elsliger Marc-André, Abdubek Polat, Agarwalla Sanjay, Ambing Eileen, Astakhova Tamara, Axelrod Herbert L, Canaves Jaume M, Carlton Dennis, Chiu Hsiu-Ju, Clayton Thomas, DiDonato Michael, Duan Lian, Feuerhelm Julie, Grittini Carina, Grzechnik Slawomir K, Hale Joanna, Hampton Eric, Haugen Justin, Jaroszewski Lukasz, Jin Kevin K, Johnson Hope, Klock Heath E, Knuth Mark W, Koesema Eric, Kreusch Andreas, Kuhn Peter, Levin Inna, McMullan Daniel, Miller Mitchell D, Morse Andrew T, Moy Kin, Nigoghossian Edward, Okach Linda, Oommachen Silvya, Page Rebecca, Paulsen Jessica, Quijano Kevin, Reyes Ron, Rife Christopher L, Sims Eric, Spraggon Glen, Sridhar Vandana, Stevens Raymond C, van den Bedem Henry, Velasquez Jeff, White Aprilfawn, Wolf Guenter, Xu Qingping, Hodgson Keith O, Wooley John, Deacon Ashley M, Godzik Adam, Lesley Scott A, Wilson Ian A

机构信息

Department of Biochemistry and Molecular Biophysics, Columbia University, New York, New York.

出版信息

Proteins. 2006 Nov 15;65(3):527-37. doi: 10.1002/prot.21130.

DOI:10.1002/prot.21130

PMID:16988933

Abstract

Glutathione S-transferases (GSTs) comprise a diverse superfamily of enzymes found in organisms from all kingdoms of life. GSTs are involved in diverse processes, notably small-molecule biosynthesis or detoxification, and are frequently also used in protein engineering studies or as biotechnology tools. Here, we report the high-resolution X-ray structure of Atu5508 from the pathogenic soil bacterium Agrobacterium tumefaciens (atGST1). Through use of comparative sequence and structural analysis of the GST superfamily, we identified local sequence and structural signatures, which allowed us to distinguish between different GST classes. This approach enables GST classification based on structure, without requiring additional biochemical or immunological data. Consequently, analysis of the atGST1 crystal structure suggests a new GST class, distinct from previously characterized GSTs, which would make it an attractive target for further biochemical studies.

摘要

谷胱甘肽S-转移酶（GSTs）是一个多样化的酶超家族，存在于所有生命王国的生物体中。GSTs参与多种过程，特别是小分子生物合成或解毒，并且经常也用于蛋白质工程研究或作为生物技术工具。在这里，我们报告了来自致病土壤细菌根癌农杆菌（atGST1）的Atu5508的高分辨率X射线结构。通过对GST超家族进行比较序列和结构分析，我们确定了局部序列和结构特征，这使我们能够区分不同的GST类别。这种方法能够基于结构对GST进行分类，而无需额外的生化或免疫学数据。因此，对atGST1晶体结构的分析表明存在一个不同于先前已表征的GST的新GST类别，这将使其成为进一步生化研究的有吸引力的目标。