Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1IPA

CRYSTAL STRUCTURE OF RNA 2'-O RIBOSE METHYLTRANSFERASE

Summary for 1IPA
Entry DOI10.2210/pdb1ipa/pdb
DescriptorRNA 2'-O-RIBOSE METHYLTRANSFERASE (2 entities in total)
Functional Keywordsdeep trefoil knot, rossmann fold, el30-like fold, riken structural genomics/proteomics initiative, rsgi, structural genomics, transferase
Biological sourceThermus thermophilus
Total number of polymer chains1
Total formula weight30017.45
Authors
Primary citationNureki, O.,Shirouzu, M.,Hashimoto, K.,Ishitani, R.,Terada, T.,Tamakoshi, M.,Oshima, T.,Chijimatsu, M.,Takio, K.,Vassylyev, D.G.,Shibata, T.,Inoue, Y.,Kuramitsu, S.,Yokoyama, S.
An enzyme with a deep trefoil knot for the active-site architecture.
Acta Crystallogr.,Sect.D, 58:1129-1137, 2002
Cited by
PubMed Abstract: Knots in polypeptide chains have been found in very few proteins. Only two proteins are considered to have a shallow 'trefoil' knot, which tucks a few residues at one end of the chain through a loop exposed on the protein surface. Recently, another protein was found by a mathematical algorithm to have a deep 'figure-of-eight' knot which had not been visually identified. In the present study, the crystal structure of a hypothetical RNA 2'-O-ribose methyltransferase from Thermus thermophilus (RrmA) was determined at 2.4 A resolution and a deep trefoil knot was found for the first time. The present knot is formed by the threading of a 44-residue polypeptide chain through a 41-residue loop and is better defined than the previously reported knots. Two of the three catalytic residues conserved in the 2'-O-ribose methyltransferase family are located in the knotting loop and in the knotted carboxy-terminal chain, which is the first observation that the enzyme active site is constructed right on the knot. On the other hand, the amino-terminal domain exhibits a geometrical similarity to the ribosomal proteins which recognize an internal loop of RNA.
PubMed: 12077432
DOI: 10.1107/S0907444902006601
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

226707

數據於2024-10-30公開中

PDB statisticsPDBj update infoContact PDBjnumon