Oganesyan Vaheh, Adams Paul D, Jancarik Jarmila, Kim Rosalind, Kim Sung-Hou
Berkeley Structural Genomics Center, Physical Biosciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 May 1;63(Pt 5):369-74. doi: 10.1107/S1744309107018945. Epub 2007 Apr 28.
Using single-wavelength anomalous dispersion data obtained from a gold-derivatized crystal, the X-ray crystal structure of the protein 067745_AQUAE from the prokaryotic organism Aquifex aeolicus has been determined to a resolution of 2.0 A. Amino-acid residues 1-371 of the 44 kDa protein were identified by Pfam as an HD domain and a member of the metal-dependent phosphohydrolase superfamily (accession No. PF01966). Although three families from this large and diverse group of enzymatic proteins are represented in the PDB, the structure of 067745_AQUAE reveals a unique fold that is unlike the others and that is likely to represent a new subfamily, further organizing the families and characterizing the proteins. Data are presented that provide the first insights into the structural organization of the proteins within this clan and a distal alternative GDP-binding domain outside the metal-binding active site is proposed.
利用从金衍生化晶体获得的单波长反常色散数据，已确定来自原核生物嗜热栖热菌的蛋白质067745_AQUAE的X射线晶体结构，分辨率为2.0埃。通过Pfam鉴定，该44 kDa蛋白质的氨基酸残基1-371为HD结构域，属于金属依赖性磷酸水解酶超家族成员（登录号PF01966）。尽管PDB中代表了这一庞大且多样的酶蛋白组中的三个家族，但067745_AQUAE的结构揭示了一种独特的折叠方式，与其他家族不同，可能代表一个新的亚家族，进一步对这些家族进行了分类并对蛋白质进行了表征。文中给出的数据首次揭示了该家族内蛋白质的结构组织情况，并提出了金属结合活性位点之外的一个远端替代性GDP结合结构域。
