STRUCTURE OF THE K7A/R10A/K66A VARIANT OF RIBONUCLEASE A

File:3rsk.gif


3rsk, resolution 2.0Å

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OverviewOverview

The active-site cleft of bovine pancreatic ribonuclease A (RNase A) is, lined with cationic residues that interact with a bound nucleic acid., Those residues interacting with the phosphoryl groups comprise the P0, P1, and P2 subsites, with the scissile P-O5' bond residing in the P1 subsite., Coulombic interactions between the P0 and P2 subsites and phosphoryl, groups of the substrate were characterized previously [Fisher, B. M., Ha, J.-H., and Raines, R. T. (1998) Biochemistry 37, 12121-12132]. Here, the, interactions between these subsites and the active-site residues His12 and, His119 are described in detail. A protein variant in which the cationic, residues in these subsites (Lys66 in the P0 subsite and Lys7 and Arg10 in, the P2 subsite) were replaced with alanine was crystallized, ... [(full description)]

About this StructureAbout this Structure

3RSK is a [Single protein] structure of sequence from [Bos taurus] with ACT as [ligand]. Active as [Pancreatic ribonuclease], with EC number [3.1.27.5]. Structure known Active Sites: B1, B2, P1 and P2. Full crystallographic information is available from [OCA].

ReferenceReference

Coulombic effects of remote subsites on the active site of ribonuclease A., Fisher BM, Schultz LW, Raines RT, Biochemistry. 1998 Dec 15;37(50):17386-401. PMID:9860854

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