2dut
From Proteopedia
(New page: 200px<br /><applet load="2dut" size="450" color="white" frame="true" align="right" spinBox="true" caption="2dut, resolution 3.0Å" /> '''Crystal structure of ...) |
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| - | [[Image:2dut.gif|left|200px]]<br /><applet load="2dut" size=" | + | [[Image:2dut.gif|left|200px]]<br /><applet load="2dut" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2dut, resolution 3.0Å" /> | caption="2dut, resolution 3.0Å" /> | ||
'''Crystal structure of a M-loop deletion variant of MENT in the native conformation'''<br /> | '''Crystal structure of a M-loop deletion variant of MENT in the native conformation'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Most serpins are associated with protease inhibition, and their ability to | + | Most serpins are associated with protease inhibition, and their ability to form loop-sheet polymers is linked to conformational disease and the human serpinopathies. Here we describe the structural and functional dissection of how a unique serpin, the non-histone architectural protein, MENT (Myeloid and Erythroid Nuclear Termination stage-specific protein), participates in DNA and chromatin condensation. Our data suggest that MENT contains at least two distinct DNA-binding sites, consistent with its simultaneous binding to the two closely juxtaposed linker DNA segments on a nucleosome. Remarkably, our studies suggest that the reactive centre loop, a region of the MENT molecule essential for chromatin bridging in vivo and in vitro, is able to mediate formation of a loop-sheet oligomer. These data provide mechanistic insight into chromatin compaction by a non-histone architectural protein and suggest how the structural plasticity of serpins has adapted to mediate physiological, rather than pathogenic, loop-sheet linkages. |
==About this Structure== | ==About this Structure== | ||
| - | 2DUT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. This structure | + | 2DUT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. This structure supersedes the now removed PDB entry 2H4S. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DUT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Gallus gallus]] | [[Category: Gallus gallus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Buckle, A | + | [[Category: Buckle, A M.]] |
| - | [[Category: Irving, J | + | [[Category: Irving, J A.]] |
[[Category: McGowan, S.]] | [[Category: McGowan, S.]] | ||
| - | [[Category: Whisstock, J | + | [[Category: Whisstock, J C.]] |
[[Category: serine protease inhibitor]] | [[Category: serine protease inhibitor]] | ||
[[Category: serpin]] | [[Category: serpin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:02:53 2008'' |
Revision as of 15:02, 21 February 2008
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Crystal structure of a M-loop deletion variant of MENT in the native conformation
Overview
Most serpins are associated with protease inhibition, and their ability to form loop-sheet polymers is linked to conformational disease and the human serpinopathies. Here we describe the structural and functional dissection of how a unique serpin, the non-histone architectural protein, MENT (Myeloid and Erythroid Nuclear Termination stage-specific protein), participates in DNA and chromatin condensation. Our data suggest that MENT contains at least two distinct DNA-binding sites, consistent with its simultaneous binding to the two closely juxtaposed linker DNA segments on a nucleosome. Remarkably, our studies suggest that the reactive centre loop, a region of the MENT molecule essential for chromatin bridging in vivo and in vitro, is able to mediate formation of a loop-sheet oligomer. These data provide mechanistic insight into chromatin compaction by a non-histone architectural protein and suggest how the structural plasticity of serpins has adapted to mediate physiological, rather than pathogenic, loop-sheet linkages.
About this Structure
2DUT is a Single protein structure of sequence from Gallus gallus. This structure supersedes the now removed PDB entry 2H4S. Full crystallographic information is available from OCA.
Reference
X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation., McGowan S, Buckle AM, Irving JA, Ong PC, Bashtannyk-Puhalovich TA, Kan WT, Henderson KN, Bulynko YA, Popova EY, Smith AI, Bottomley SP, Rossjohn J, Grigoryev SA, Pike RN, Whisstock JC, EMBO J. 2006 Jul 12;25(13):3144-55. Epub 2006 Jun 29. PMID:16810322
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