1rls
From Proteopedia
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'''CRYSTAL STRUCTURE OF RNASE T1 COMPLEXED WITH THE PRODUCT NUCLEOTIDE 3'-GMP. STRUCTURAL EVIDENCE FOR DIRECT INTERACTION OF HISTIDINE 40 AND GLUTAMIC ACID 58 WITH THE 2'-HYDROXYL GROUP OF RIBOSE''' | '''CRYSTAL STRUCTURE OF RNASE T1 COMPLEXED WITH THE PRODUCT NUCLEOTIDE 3'-GMP. STRUCTURAL EVIDENCE FOR DIRECT INTERACTION OF HISTIDINE 40 AND GLUTAMIC ACID 58 WITH THE 2'-HYDROXYL GROUP OF RIBOSE''' | ||
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Crystal structure of RNase T1 complexed with the product nucleotide 3'-GMP. Structural evidence for direct interaction of histidine 40 and glutamic acid 58 with the 2'-hydroxyl group of the ribose., Gohda K, Oka K, Tomita K, Hakoshima T, J Biol Chem. 1994 Jul 1;269(26):17531-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7912696 7912696] | Crystal structure of RNase T1 complexed with the product nucleotide 3'-GMP. Structural evidence for direct interaction of histidine 40 and glutamic acid 58 with the 2'-hydroxyl group of the ribose., Gohda K, Oka K, Tomita K, Hakoshima T, J Biol Chem. 1994 Jul 1;269(26):17531-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7912696 7912696] | ||
[[Category: Aspergillus oryzae]] | [[Category: Aspergillus oryzae]] | ||
| - | [[Category: Ribonuclease T(1)]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Gohda, K.]] | [[Category: Gohda, K.]] | ||
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[[Category: Oka, K I.]] | [[Category: Oka, K I.]] | ||
[[Category: Tomita, K I.]] | [[Category: Tomita, K I.]] | ||
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Revision as of 04:39, 3 May 2008
CRYSTAL STRUCTURE OF RNASE T1 COMPLEXED WITH THE PRODUCT NUCLEOTIDE 3'-GMP. STRUCTURAL EVIDENCE FOR DIRECT INTERACTION OF HISTIDINE 40 AND GLUTAMIC ACID 58 WITH THE 2'-HYDROXYL GROUP OF RIBOSE
Overview
The crystal structure of RNase T1 complexed with 3'-GMP has been determined. The glycosyl conformation of 3'-GMP is in the syn conformation, and the ribose adopts the O4'-endo pucker. This observed pucker is different from that in any complex structures of RNase T1. In the present complex, this energetically unfavorable conformation is stabilized by the water molecule with the bridged hydrogen bonds between the O2' and the O3' atoms of the ribose. The guanine base is recognized in the same manner as observed in the complex of 2'-GMP. The 2'-hydroxyl group of the ribose shows a tight hydrogen bond to both His-40 and Glu-58 with the suitable geometry for the proton transfer. These hydrogen bonds suggest that the two residues can participate directly in the proton transfer. His-92 is hydrogen bonded to two the proton transfer. His-92 is hydrogen bonded to two oxygen atoms of the phosphate group. Based on the geometry in the active site, the O1P atom may correspond to the O5' atom of the leaving nucleotide in the phosphoryl transfer or a water molecule as a nucleophile in the hydrolysis reaction. In the present complex, the conformations of the 3'-GMP molecule and the side chains of the catalytic residues would be represented as the conformation before the phosphoryl transfer reaction and/or after the hydrolysis reaction.
About this Structure
1RLS is a Single protein structure of sequence from Aspergillus oryzae. Full crystallographic information is available from OCA.
Reference
Crystal structure of RNase T1 complexed with the product nucleotide 3'-GMP. Structural evidence for direct interaction of histidine 40 and glutamic acid 58 with the 2'-hydroxyl group of the ribose., Gohda K, Oka K, Tomita K, Hakoshima T, J Biol Chem. 1994 Jul 1;269(26):17531-6. PMID:7912696 Page seeded by OCA on Sat May 3 07:39:13 2008
