1nrf
From Proteopedia
(New page: 200px<br /><applet load="1nrf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nrf, resolution 2.50Å" /> '''C-terminal domain of...) |
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| - | [[Image:1nrf.gif|left|200px]]<br /><applet load="1nrf" size=" | + | [[Image:1nrf.gif|left|200px]]<br /><applet load="1nrf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nrf, resolution 2.50Å" /> | caption="1nrf, resolution 2.50Å" /> | ||
'''C-terminal domain of the Bacillus licheniformis BlaR penicillin-receptor'''<br /> | '''C-terminal domain of the Bacillus licheniformis BlaR penicillin-receptor'''<br /> | ||
==Overview== | ==Overview== | ||
| - | As in several staphylococci, the synthesis of the Bacillus licheniformis | + | As in several staphylococci, the synthesis of the Bacillus licheniformis 749/I beta-lactamase is an inducible phenomenon regulated by a signal-transducing membrane protein BlaR. The C-terminal domain of this multimodular protein is an extracellular domain which specifically recognizes beta-lactam antibiotics. When it binds a beta-lactam, a signal is transmitted by the transmembrane region to the intracellular loops. In response, the hydrolytic activity of the BlaR large cytoplasmic L3 loop is induced, and a cascade of reactions is generated, leading to the transcription of the beta-lactamase gene. Here, we describe the crystal structure of the extracellular penicillin-receptor domain of BlaR (residues 346-601) at 2.5 A resolution in order to understand why this domain, whose folding is very similar to that of class D beta-lactamases, behaves as a highly sensitive penicillin-binding protein rather than a beta-lactamase. Two residues of the BlaR C-terminal domain, Thr452 and Thr542, modify the hydrophobic characteristic of the class D beta-lactamase active site. Both residues seem to be in part responsible for the lack of beta-lactamase activity of the BlaR protein due to the stability of the acyl-enzyme. Although further experimental data are needed to fully understand the transmembrane induction process, the comparison of the BlaR sensor domain structure with those of class D beta-lactamase complexes and penicillin-binding proteins provides interesting elements to hypothesize on possible signal transmission mechanisms. |
==About this Structure== | ==About this Structure== | ||
| - | 1NRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_licheniformis Bacillus licheniformis]. Full crystallographic information is available from [http:// | + | 1NRF is a [http://en.wikipedia.org/wiki/Single_protein 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=1NRF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Brans, A.]] | [[Category: Brans, A.]] | ||
[[Category: Charlier, P.]] | [[Category: Charlier, P.]] | ||
| - | [[Category: Columbo, M | + | [[Category: Columbo, M L.]] |
[[Category: Fonze, E.]] | [[Category: Fonze, E.]] | ||
| - | [[Category: Frere, J | + | [[Category: Frere, J M.]] |
[[Category: Joris, B.]] | [[Category: Joris, B.]] | ||
[[Category: Kerff, F.]] | [[Category: Kerff, F.]] | ||
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[[Category: penicillin-receptor]] | [[Category: penicillin-receptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:12 2008'' |
Revision as of 12:09, 21 February 2008
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C-terminal domain of the Bacillus licheniformis BlaR penicillin-receptor
Overview
As in several staphylococci, the synthesis of the Bacillus licheniformis 749/I beta-lactamase is an inducible phenomenon regulated by a signal-transducing membrane protein BlaR. The C-terminal domain of this multimodular protein is an extracellular domain which specifically recognizes beta-lactam antibiotics. When it binds a beta-lactam, a signal is transmitted by the transmembrane region to the intracellular loops. In response, the hydrolytic activity of the BlaR large cytoplasmic L3 loop is induced, and a cascade of reactions is generated, leading to the transcription of the beta-lactamase gene. Here, we describe the crystal structure of the extracellular penicillin-receptor domain of BlaR (residues 346-601) at 2.5 A resolution in order to understand why this domain, whose folding is very similar to that of class D beta-lactamases, behaves as a highly sensitive penicillin-binding protein rather than a beta-lactamase. Two residues of the BlaR C-terminal domain, Thr452 and Thr542, modify the hydrophobic characteristic of the class D beta-lactamase active site. Both residues seem to be in part responsible for the lack of beta-lactamase activity of the BlaR protein due to the stability of the acyl-enzyme. Although further experimental data are needed to fully understand the transmembrane induction process, the comparison of the BlaR sensor domain structure with those of class D beta-lactamase complexes and penicillin-binding proteins provides interesting elements to hypothesize on possible signal transmission mechanisms.
About this Structure
1NRF is a Single protein structure of sequence from Bacillus licheniformis. Full crystallographic information is available from OCA.
Reference
Crystal structure of the sensor domain of the BlaR penicillin receptor from Bacillus licheniformis., Kerff F, Charlier P, Colombo ML, Sauvage E, Brans A, Frere JM, Joris B, Fonze E, Biochemistry. 2003 Nov 11;42(44):12835-43. PMID:14596597
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