2h4q
From Proteopedia
|
Crystal structure of a M-loop deletion variant of MENT in the cleaved 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
2H4Q is a Protein complex structure of sequences from Gallus gallus. 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
Page seeded by OCA on Tue Jan 29 20:14:22 2008
