2H4R: Crystal Structure Of Wildtype Ment In The Native Conformation

Citation:
Abstract
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.
PDB ID: 2H4RDownload
MMDB ID: 40521
PDB Deposition Date: 2006/5/25
Updated in MMDB: 2012/11
Experimental Method:
x-ray diffraction
Resolution: 2.7  Å
Source Organism:
Similar Structures:
Biological Unit for 2H4R: monomeric; determined by author
Molecular Components in 2H4R
Label Count Molecule
Protein (1 molecule)
1
Heterochromatin-associated Protein Ment(Gene symbol: SERPINB10B)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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