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1a2w
From Proteopedia
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Revision as of 12:39, 30 October 2007
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CRYSTAL STRUCTURE OF A 3D DOMAIN-SWAPPED DIMER OF BOVINE PANCREATIC RIBONUCLEASE A
Overview
The dimer of bovine pancreatic ribonuclease A (RNase A) discovered by, Crestfield, Stein, and Moore in 1962 has been crystallized and its, structure determined and refined to a 2.1-A resolution. The dimer is 3D, domain-swapped. The N-terminal helix (residues 1-15) of each subunit is, swapped into the major domain (residues 23-124) of the other subunit. The, dimer of bull seminal ribonuclease (BS-RNase) is also known to be, domain-swapped, but the relationship of the subunits within the two dimers, is strikingly different. In the RNase A dimer, the 3-stranded beta sheets, of the two subunits are hydrogen-bonded at their edges to form a, continuous 6-stranded sheet across the dimer interface; in the BS-RNase, dimer, it is instead the two helices that abut. Whereas the BS-RNase dimer, has ... [(full description)]
About this Structure
1A2W is a [Single protein] structure of sequence from [Bos taurus] with CL and SO4 as [ligands]. Active as [Pancreatic ribonuclease], with EC number [3.1.27.5]. Structure known Active Site: AVE. Full crystallographic information is available from [OCA].
Reference
The crystal structure of a 3D domain-swapped dimer of RNase A at a 2.1-A resolution., Liu Y, Hart PJ, Schlunegger MP, Eisenberg D, Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3437-42. PMID:9520384
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