1p6r: Difference between revisions

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[[Image:1p6r.jpg|left|200px]]<br /><applet load="1p6r" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1p6r.jpg|left|200px]]<br /><applet load="1p6r" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1p6r" />

'''Solution structure of the DNA binding domain of the repressor BlaI.'''<br />

==Overview==

beta-Lactamase and penicillin-binding protein PBP2' mediate staphylococcal, resistance to beta-lactam antibiotics, which are otherwise highly, clinically effective. Two repressors (BlaI and MecI) regulate expression, of these inducible proteins. Here, we present the first solution structure, of the 82 amino acid residue DNA-binding domain of Bacillus licheniformis, BlaI which is very similar in primary sequence to the medically, significant Staphyloccocal BlaI and MecI proteins. This structure is, composed of a compact core of three alpha-helices and a three-stranded, beta-sheet typical of the winged helix protein (WHP) family. The, protein/DNA complex was studied by NMR chemical shift comparison between, the free and complexed forms of BlaI. Residues involved in DNA interaction, were identified and a WHP canonical model of interaction with the, operators is proposed. In this model, specific contacts occur between the, base-pairs of the TACA motif and conserved amino acid residues of the, repressor helix H3. These results help toward understanding the repression, and induction mechanism of the genes coding for beta-lactamase and PBP2'.

beta-Lactamase and penicillin-binding protein PBP2' mediate staphylococcal resistance to beta-lactam antibiotics, which are otherwise highly clinically effective. Two repressors (BlaI and MecI) regulate expression of these inducible proteins. Here, we present the first solution structure of the 82 amino acid residue DNA-binding domain of Bacillus licheniformis BlaI which is very similar in primary sequence to the medically significant Staphyloccocal BlaI and MecI proteins. This structure is composed of a compact core of three alpha-helices and a three-stranded beta-sheet typical of the winged helix protein (WHP) family. The protein/DNA complex was studied by NMR chemical shift comparison between the free and complexed forms of BlaI. Residues involved in DNA interaction were identified and a WHP canonical model of interaction with the operators is proposed. In this model, specific contacts occur between the base-pairs of the TACA motif and conserved amino acid residues of the repressor helix H3. These results help toward understanding the repression and induction mechanism of the genes coding for beta-lactamase and PBP2'.

==About this Structure==

1P6R 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1P6R OCA].

1P6R 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=1P6R OCA].

==Reference==

Line 17:

[[Category: Joris, B.]]

[[Category: Llabres, G.]]

[[Category: Melckebeke, H.V.]]

[[Category: Melckebeke, H V.]]

[[Category: Simorre, J.P.]]

[[Category: Simorre, J P.]]

[[Category: Vreuls, C.]]

[[Category: bacterial resistance to antibiotics]]

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[[Category: winged helix protein]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:44 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1p6r.jpg|left|200px]]<br /><applet load="1p6r" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1p6r.jpg|left|200px]]<br /><applet load="1p6r" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1p6r" />
 '''Solution structure of the DNA binding domain of the repressor BlaI.'''<br />
 ==Overview==
-beta-Lactamase and penicillin-binding protein PBP2' mediate staphylococcal, resistance to beta-lactam antibiotics, which are otherwise highly, clinically effective. Two repressors (BlaI and MecI) regulate expression, of these inducible proteins. Here, we present the first solution structure, of the 82 amino acid residue DNA-binding domain of Bacillus licheniformis, BlaI which is very similar in primary sequence to the medically, significant Staphyloccocal BlaI and MecI proteins. This structure is, composed of a compact core of three alpha-helices and a three-stranded, beta-sheet typical of the winged helix protein (WHP) family. The, protein/DNA complex was studied by NMR chemical shift comparison between, the free and complexed forms of BlaI. Residues involved in DNA interaction, were identified and a WHP canonical model of interaction with the, operators is proposed. In this model, specific contacts occur between the, base-pairs of the TACA motif and conserved amino acid residues of the, repressor helix H3. These results help toward understanding the repression, and induction mechanism of the genes coding for beta-lactamase and PBP2'.
+beta-Lactamase and penicillin-binding protein PBP2' mediate staphylococcal resistance to beta-lactam antibiotics, which are otherwise highly clinically effective. Two repressors (BlaI and MecI) regulate expression of these inducible proteins. Here, we present the first solution structure of the 82 amino acid residue DNA-binding domain of Bacillus licheniformis BlaI which is very similar in primary sequence to the medically significant Staphyloccocal BlaI and MecI proteins. This structure is composed of a compact core of three alpha-helices and a three-stranded beta-sheet typical of the winged helix protein (WHP) family. The protein/DNA complex was studied by NMR chemical shift comparison between the free and complexed forms of BlaI. Residues involved in DNA interaction were identified and a WHP canonical model of interaction with the operators is proposed. In this model, specific contacts occur between the base-pairs of the TACA motif and conserved amino acid residues of the repressor helix H3. These results help toward understanding the repression and induction mechanism of the genes coding for beta-lactamase and PBP2'.
 ==About this Structure==
-P6R 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P6R OCA].
+P6R 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=1P6R OCA].
 ==Reference==
@@ Line 17: / Line 17: @@
 [[Category: Joris, B.]]
 [[Category: Llabres, G.]]
-[[Category: Melckebeke, H.V.]]
+[[Category: Melckebeke, H V.]]
-[[Category: Simorre, J.P.]]
+[[Category: Simorre, J P.]]
 [[Category: Vreuls, C.]]
 [[Category: bacterial resistance to antibiotics]]
@@ Line 26: / Line 26: @@
 [[Category: winged helix protein]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:31:41 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:44 2008''