1WDV

Crystal structure of hypothetical protein APE2540

Summary for 1WDV

• Entry DOI: 10.2210/pdb1wdv/pdb
• Descriptor: hypothetical protein APE2540 (2 entities in total)
• Functional Keywords: structural genomics, unknown function, riken structural genomics/proteomics initiative, rsgi
• Biological source: Aeropyrum pernix
• Total number of polymer chains: 2
• Total formula weight: 32961.63

Authors

Murayama, K.,Kato-Murayama, M.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-05-18, release date: 2004-11-18, Last modification date: 2024-10-30)

Primary citation

Murayama, K.,Kato-Murayama, M.,Katsura, K.,Uchikubo-Kamo, T.,Yamaguchi-Hirafuji, M.,Kawazoe, M.,Akasaka, R.,Hanawa-Suetsugu, K.,Hori-Takemoto, C.,Terada, T.,Shirouzu, M.,Yokoyama, S.
Structure of a putative trans-editing enzyme for prolyl-tRNA synthetase from Aeropyrum pernix K1 at 1.7 A resolution.
Acta Crystallogr.,Sect.F, 61:26-29, 2005

PubMed Abstract: The crystal structure of APE2540, the putative trans-editing enzyme ProX from Aeropyrum pernix K1, was determined in a high-throughput manner. The crystal belongs to the monoclinic space group P2(1), with unit-cell parameters a = 47.4, b = 58.9, c = 53.6 A, beta = 106.8 degrees. The structure was solved by the multiwavelength anomalous dispersion method at 1.7 A and refined to an R factor of 16.8% (Rfree = 20.5%). The crystal structure includes two protein molecules in the asymmetric unit. Each monomer consists of eight beta-strands and seven alpha-helices. A structure-homology search revealed similarity between the trans-editing enzyme YbaK (or cysteinyl-tRNAPro deacylase) from Haemophilus influenzae (HI1434; 22% sequence identity) and putative ProX proteins from Caulobacter crescentus (16%) and Agrobacterium tumefaciens (21%).

PubMed: 16508081
DOI: 10.1107/S1744309104032555

Experimental method

X-RAY DIFFRACTION (1.7 Å)