1l1m: Difference between revisions

Revision as of 14:40, 21 February 2008

SOLUTION STRUCTURE OF A DIMER OF LAC REPRESSOR DNA-BINDING DOMAIN COMPLEXED TO ITS NATURAL OPERATOR O1

OverviewOverview

The lac repressor-operator system is a model system for understanding protein-DNA interactions and allosteric mechanisms in gene regulation. Despite the wealth of biochemical data provided by extensive mutations of both repressor and operator, the specific recognition mechanism of the natural lac operators by lac repressor has remained elusive. Here we present the first high-resolution structure of a dimer of the DNA-binding domain of lac repressor bound to its natural operator 01. The global positioning of the dimer on the operator is dramatically asymmetric, which results in a different pattern of specific contacts between the two sites. Specific recognition is accomplished by a combination of elongation and twist by 48 degrees of the right lac subunit relative to the left one, significant rearrangement of many side chains as well as sequence-dependent deformability of the DNA. The set of recognition mechanisms involved in the lac repressor-operator system is unique among other protein-DNA complexes and presents a nice example of the adaptability that both proteins and DNA exhibit in the context of their mutual interaction.

About this StructureAbout this Structure

1L1M is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

ReferenceReference

Plasticity in protein-DNA recognition: lac repressor interacts with its natural operator 01 through alternative conformations of its DNA-binding domain., Kalodimos CG, Bonvin AM, Salinas RK, Wechselberger R, Boelens R, Kaptein R, EMBO J. 2002 Jun 17;21(12):2866-76. PMID:12065400

Page seeded by OCA on Thu Feb 21 13:40:17 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1l1m.gif|left|200px]]<br /><applet load="1l1m" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1l1m.gif|left|200px]]<br /><applet load="1l1m" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1l1m" />
 '''SOLUTION STRUCTURE OF A DIMER OF LAC REPRESSOR DNA-BINDING DOMAIN COMPLEXED TO ITS NATURAL OPERATOR O1'''<br />
 ==Overview==
-The lac repressor-operator system is a model system for understanding, protein-DNA interactions and allosteric mechanisms in gene regulation., Despite the wealth of biochemical data provided by extensive mutations of, both repressor and operator, the specific recognition mechanism of the, natural lac operators by lac repressor has remained elusive. Here we, present the first high-resolution structure of a dimer of the DNA-binding, domain of lac repressor bound to its natural operator 01. The global, positioning of the dimer on the operator is dramatically asymmetric, which, results in a different pattern of specific contacts between the two sites., Specific recognition is accomplished by a combination of elongation and, twist by 48 degrees of the right lac subunit relative to the left one, significant rearrangement of many side chains as well as, sequence-dependent deformability of the DNA. The set of recognition, mechanisms involved in the lac repressor-operator system is unique among, other protein-DNA complexes and presents a nice example of the, adaptability that both proteins and DNA exhibit in the context of their, mutual interaction.
+The lac repressor-operator system is a model system for understanding protein-DNA interactions and allosteric mechanisms in gene regulation. Despite the wealth of biochemical data provided by extensive mutations of both repressor and operator, the specific recognition mechanism of the natural lac operators by lac repressor has remained elusive. Here we present the first high-resolution structure of a dimer of the DNA-binding domain of lac repressor bound to its natural operator 01. The global positioning of the dimer on the operator is dramatically asymmetric, which results in a different pattern of specific contacts between the two sites. Specific recognition is accomplished by a combination of elongation and twist by 48 degrees of the right lac subunit relative to the left one, significant rearrangement of many side chains as well as sequence-dependent deformability of the DNA. The set of recognition mechanisms involved in the lac repressor-operator system is unique among other protein-DNA complexes and presents a nice example of the adaptability that both proteins and DNA exhibit in the context of their mutual interaction.
 ==About this Structure==
-L1M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L1M OCA].
+L1M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L1M OCA].
 ==Reference==
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 [[Category: Single protein]]
 [[Category: Boelens, R.]]
-[[Category: Bonvin, A.M.J.J.]]
+[[Category: Bonvin, A M.J J.]]
-[[Category: Kalodimos, C.G.]]
+[[Category: Kalodimos, C G.]]
 [[Category: Kaptein, R.]]
-[[Category: Salinas, R.K.]]
+[[Category: Salinas, R K.]]
 [[Category: Wechselberger, R.]]
 [[Category: asymmetric dna-binding]]
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 [[Category: transcription regulation]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:10:10 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:40:17 2008''