1V9F

Crystal structure of catalytic domain of pseudouridine synthase RluD from Escherichia coli

Summary for 1V9F

• Entry DOI: 10.2210/pdb1v9f/pdb
• Descriptor: Ribosomal large subunit pseudouridine synthase D, PHOSPHATE ION (3 entities in total)
• Functional Keywords: pseudouridine synthase, rna binding, lyase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 37144.43

Authors

Mizutani, K.,Machida, Y.,Unzai, S.,Park, S.-Y.,Tame, J.R.H. (deposition date: 2004-01-26, release date: 2004-05-18, Last modification date: 2023-12-27)

Primary citation

Mizutani, K.,Machida, Y.,Unzai, S.,Park, S.-Y.,Tame, J.R.H.
Crystal structures of the catalytic domains of pseudouridine synthases RluC and RluD from Escherichia coli
Biochemistry, 43:4454-4463, 2004

PubMed Abstract: The most frequent modification of RNA, the conversion of uridine bases to pseudouridines, is found in all living organisms and often in highly conserved locations in ribosomal and transfer RNA. RluC and RluD are homologous enzymes which each convert three specific uridine bases in Escherichia coli ribosomal 23S RNA to pseudouridine: bases 955, 2504, and 2580 in the case of RluC and 1911, 1915, and 1917 in the case of RluD. Both have an N-terminal S4 RNA binding domain. While the loss of RluC has little phenotypic effect, loss of RluD results in a much reduced growth rate. We have determined the crystal structures of the catalytic domain of RluC, and full-length RluD. The S4 domain of RluD appears to be highly flexible or unfolded and is completely invisible in the electron density map. Despite the conserved topology shared by the two proteins, the surface shape and charge distribution are very different. The models suggest significant differences in substrate binding by different pseudouridine synthases.

PubMed: 15078091
DOI: 10.1021/bi036079c

Experimental method

X-RAY DIFFRACTION (1.7 Å)