1uhm: Difference between revisions

Revision as of 18:08, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1uhm.png

Template:STRUCTURE 1uhm

Solution structure of the globular domain of linker histone homolog Hho1p from S. cerevisiaeSolution structure of the globular domain of linker histone homolog Hho1p from S. cerevisiae

Template:ABSTRACT PUBMED 14654695

About this StructureAbout this Structure

1UHM is a Single protein structure of sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA.

ReferenceReference

The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy., Ono K, Kusano O, Shimotakahara S, Shimizu M, Yamazaki T, Shindo H, Nucleic Acids Res. 2003 Dec 15;31(24):7199-207. PMID:14654695

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-'''Solution structure of the globular domain of linker histone homolog Hho1p from S. cerevisiae'''
+===Solution structure of the globular domain of linker histone homolog Hho1p from S. cerevisiae===
-==Overview==
+<!--
-Hho1p is assumed to serve as a linker histone in Saccharomyces cerevisiae and, notably, it possesses two putative globular domains, designated HD1 (residues 41-118) and HD2 (residues 171-252), that are homologous to histone H5 from chicken erythrocytes. We have determined the three-dimensional structure of globular domain HD1 with high precision by heteronuclear magnetic resonance spectroscopy. The structure had a winged helix-turn-helix motif composed of an alphabetaalphaalphabetabeta fold and closely resembled the structure of the globular domain of histone H5. Interestingly, the second globular domain, HD2, in Hho1p was unstructured under physiological conditions. Gel mobility assay demonstrated that Hho1p preferentially binds to supercoiled DNA over linearized DNA. Furthermore, NMR analysis of the complex of a deletion mutant protein (residues 1-118) of Hho1p with a linear DNA duplex revealed that four regions within the globular domain HD1 are involved in the DNA binding. The above results suggested that Hho1p possesses properties similar to those of linker histones in higher eukaryotes in terms of the structure and binding preference towards supercoiled DNA.
+The line below this paragraph, {{ABSTRACT_PUBMED_14654695}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14654695 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_14654695}}
 ==About this Structure==
-UHM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UHM OCA].
+UHM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UHM OCA].
 ==Reference==
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 [[Category: Structural genomic]]
 [[Category: Winged helix-turn-helix]]
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