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2p7c

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[[Image:2p7c.gif|left|200px]]
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[[Image:2p7c.png|left|200px]]
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{{STRUCTURE_2p7c| PDB=2p7c | SCENE= }}
{{STRUCTURE_2p7c| PDB=2p7c | SCENE= }}
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'''Solution structure of the bacillus licheniformis BlaI monomeric form in complex with the blaP half-operator.'''
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===Solution structure of the bacillus licheniformis BlaI monomeric form in complex with the blaP half-operator.===
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==Overview==
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In absence of beta-lactam antibiotics, BlaI and MecI homodimeric repressors negatively control the expression of genes involved in beta-lactam resistance in Bacillus licheniformis and in Staphylococcus aureus. Subsequently to beta-lactam presence, BlaI/MecI is inactivated by a single-point proteolysis that separates its N-terminal DNA-binding domain to its C-terminal domain responsible for its dimerization. Concomitantly to this proteolysis, the truncated repressor acquires a low affinity for its DNA target that explains the expression of the structural gene for resistance. To understand the loss of the high DNA affinity of the truncated repressor, we have determined the different dissociation constants of the system and solved the solution structure of the B. licheniformis monomeric repressor complexed to the semi-operating sequence OP1 of blaP (1/2OP1blaP) by using a de novo docking approach based on inter-molecular nuclear Overhauser effects and chemical-shift differences measured on each macromolecular partner. Although the N-terminal domain of the repressor is not subject to internal structural rearrangements upon DNA binding, the molecules adopt a tertiary conformation different from the crystallographic operator-repressor dimer complex, leading to a 30 degrees rotation of the monomer with respect to a central axis extended across the DNA. These results open new insights for the repression and induction mechanisms of bacterial resistance to beta-lactams.
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(as it appears on PubMed at http://www.pubmed.gov), where 17576674 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17576674}}
==About this Structure==
==About this Structure==
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2P7C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P7C OCA].
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2P7C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P7C OCA].
==Reference==
==Reference==
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[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
[[Category: Repressor]]
[[Category: Repressor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:32:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:39:53 2008''

Revision as of 00:39, 29 July 2008

Image:2p7c.png

Template:STRUCTURE 2p7c

Solution structure of the bacillus licheniformis BlaI monomeric form in complex with the blaP half-operator.

Template:ABSTRACT PUBMED 17576674

About this Structure

2P7C is a Single protein structure of sequence from Bacillus licheniformis. Full experimental information is available from OCA.

Reference

Conformational and thermodynamic changes of the repressor/DNA operator complex upon monomerization shed new light on regulation mechanisms of bacterial resistance against beta-lactam antibiotics., Boudet J, Duval V, Van Melckebeke H, Blackledge M, Amoroso A, Joris B, Simorre JP, Nucleic Acids Res. 2007;35(13):4384-95. Epub 2007 Jun 18. PMID:17576674

Page seeded by OCA on Tue Jul 29 03:39:53 2008

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