Bakolitsa Constantina, Bateman Alex, Jin Kevin K, McMullan Daniel, Krishna S Sri, Miller Mitchell D, Abdubek Polat, Acosta Claire, Astakhova Tamara, Axelrod Herbert L, Burra Prasad, Carlton Dennis, Chiu Hsiu Ju, Clayton Thomas, Das Debanu, Deller Marc C, Duan Lian, Elias Ylva, Feuerhelm Julie, Grant Joanna C, Grzechnik Anna, Grzechnik Slawomir K, Han Gye Won, Jaroszewski Lukasz, Klock Heath E, Knuth Mark W, Kozbial Piotr, Kumar Abhinav, Marciano David, Morse Andrew T, Murphy Kevin D, Nigoghossian Edward, Okach Linda, Oommachen Silvya, Paulsen Jessica, Reyes Ron, Rife Christopher L, Sefcovic Natasha, Tien Henry, Trame Christine B, Trout Christina V, van den Bedem Henry, Weekes Dana, White Aprilfawn, Xu Qingping, Hodgson Keith O, Wooley John, Elsliger Marc André, Deacon Ashley M, Godzik Adam, Lesley Scott, Wilson Ian A
Stanford Synchrotron Radiation Lightsource, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Oct 1;66(Pt 10):1198-204. doi: 10.1107/S1744309109025196. Epub 2009 Oct 27.
The crystal structure of Jann_2411 from Jannaschia sp. strain CCS1, a member of the Pfam PF07336 family classified as a domain of unknown function (DUF1470), was solved to a resolution of 1.45 Å by multiple-wavelength anomalous dispersion (MAD). This protein is the first structural representative of the DUF1470 Pfam family. Structural analysis revealed a two-domain organization, with the N-terminal domain presenting a new fold called the ABATE domain that may bind an as yet unknown ligand. The C-terminal domain forms a treble-clef zinc finger that is likely to be involved in DNA binding. Analysis of the Jann_2411 protein and the broader ABATE-domain family suggests a role as stress-induced transcriptional regulators.
来自詹氏菌属菌株CCS1的Jann_2411的晶体结构已通过多波长反常色散（MAD）法解析到1.45 Å的分辨率。Jann_2411是被归类为未知功能结构域（DUF1470）的Pfam PF07336家族的成员。该蛋白是DUF1470 Pfam家族的首个结构代表。结构分析揭示了一种双结构域组织，其中N端结构域呈现出一种名为ABATE结构域的新折叠，可能结合一种未知配体。C端结构域形成一个三叶草形锌指，可能参与DNA结合。对Jann_2411蛋白和更广泛的ABATE结构域家族的分析表明其作为应激诱导转录调节因子的作用。
