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| - | [[Image:11bg.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_11bg| PDB=11bg | SCENE= }} | | {{STRUCTURE_11bg| PDB=11bg | SCENE= }} |
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| - | '''A POTENTIAL ALLOSTERIC SUBSITE GENERATED BY DOMAIN SWAPPING IN BOVINE SEMINAL RIBONUCLEASE'''
| + | ===A POTENTIAL ALLOSTERIC SUBSITE GENERATED BY DOMAIN SWAPPING IN BOVINE SEMINAL RIBONUCLEASE=== |
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| - | ==Overview==
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| - | Bovine seminal ribonuclease (BS-RNase) is a peculiar member of the pancreatic-like ribonuclease superfamily endowed with unique biological functions. It has been shown that native BS-RNase is a mixture of two distinct dimeric forms. The most abundant form is characterised by the swapping of the N-terminal helix. Kinetic studies have shown that this dimer is allosterically regulated, whereas the minor component, in which no swapping occurs, exhibits typical Michaelian kinetics. In order to correlate the catalytic properties with the structural features of BS-RNase, we have determined the crystal structure of the BS-RNase swapping dimer complexed with uridylyl(2'-5')guanosine. The structure of the complex was refined to an R value of 0.189 at 1.9 A resolution. Surprisingly, the enzyme binds four dinucleotide molecules, all in a non-productive way. In the two active sites, the guanine base is located in the subsite that is specific for pyrimidines. This unusual binding has been observed also in complexes of RNase A with guanine-containing nucleotides (retro-binding). One of the two additional dinucleotide molecules bound to the enzyme is located on the surface of the protein in a pocket generated by crystal packing; the second was found in a cavity at the interface between the two subunits of the swapping dimer. There are indications that the interface site plays a role in the allosteric regulation exhibited by BS-RNase. This finding suggests that domain swapping may not merely be a mechanism that proteins adopt for the transition from a monomeric to oligomeric state but can be used to achieve modulations in catalytic function.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_10543951}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 10543951 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_10543951}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Phosphoric diester]] | | [[Category: Phosphoric diester]] |
| | [[Category: Rna]] | | [[Category: Rna]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:27:21 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:24:40 2008'' |
Revision as of 12:24, 30 June 2008
Template:STRUCTURE 11bg
A POTENTIAL ALLOSTERIC SUBSITE GENERATED BY DOMAIN SWAPPING IN BOVINE SEMINAL RIBONUCLEASE
Template:ABSTRACT PUBMED 10543951
About this Structure
11BG is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
A potential allosteric subsite generated by domain swapping in bovine seminal ribonuclease., Vitagliano L, Adinolfi S, Sica F, Merlino A, Zagari A, Mazzarella L, J Mol Biol. 1999 Oct 29;293(3):569-77. PMID:10543951
Page seeded by OCA on Mon Jun 30 15:24:40 2008
