1r5c: Difference between revisions

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{{STRUCTURE_1r5c|  PDB=1r5c  |  SCENE=  }}  
{{STRUCTURE_1r5c|  PDB=1r5c  |  SCENE=  }}  


'''X-ray structure of the complex of Bovine seminal ribonuclease swapping dimer with d(CpA)'''
===X-ray structure of the complex of Bovine seminal ribonuclease swapping dimer with d(CpA)===




==Overview==
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Bovine seminal ribonuclease (BS-RNase) is a unique member of the pancreatic-like ribonuclease superfamily. This enzyme exists as two conformational isomers with distinctive biological properties. The structure of the major isomer is characterized by the swapping of the N-terminal segment (MxM BS-RNase). In this article, the crystal structures of the ligand-free MxM BS-RNase and its complex with 2'-deoxycitidylyl(3',5')-2'-deoxyadenosine derived from isomorphous crystals have been refined. Interestingly, the comparison between this novel ligand-free form and the previously published sulfate-bound structure reveals significant differences. In particular, the ligand-free MxM BS-RNase is closer to the structure of MxM BS-RNase productive complexes than to the sulfate-bound form. These results reveal that MxM BS-RNase presents a remarkable flexibility, despite the structural constraints of the interchain disulfide bridges and the swapping of the N-terminal helices. These findings have important implications to the ligand binding mechanism of MxM BS-RNase. Indeed, a population shift rather than a substrate-induced conformational transition may occur in the MxM BS-RNase ligand binding process.
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{{ABSTRACT_PUBMED_15048772}}


==About this Structure==
==About this Structure==
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[[Category: Ribonuclease]]
[[Category: Ribonuclease]]
[[Category: X-ray diffraction]]
[[Category: X-ray diffraction]]
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