1uhm

From Proteopedia

(Difference between revisions)

Revision as of 06:45, 2 March 2022

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

Structural highlights

1uhm is a 1 chain structure with sequence from Atcc 18824. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	HHO1 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[H1_YEAST] Could act as an H1-type linker histone. Has been shown to bind DNA.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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 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^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Landsman D. Histone H1 in Saccharomyces cerevisiae: a double mystery solved? Trends Biochem Sci. 1996 Aug;21(8):287-8. PMID:8772381
↑ Ushinsky SC, Bussey H, Ahmed AA, Wang Y, Friesen J, Williams BA, Storms RK. Histone H1 in Saccharomyces cerevisiae. Yeast. 1997 Feb;13(2):151-61. PMID:9046096 doi:<151::AID-YEA94>3.0.CO;2-5 http://dx.doi.org/10.1002/(SICI)1097-0061(199702)13:2<151::AID-YEA94>3.0.CO;2-5
↑ Ono K, Kusano O, Shimotakahara S, Shimizu M, Yamazaki T, Shindo H. The linker histone homolog Hho1p from Saccharomyces cerevisiae represents a winged helix-turn-helix fold as determined by NMR spectroscopy. Nucleic Acids Res. 2003 Dec 15;31(24):7199-207. PMID:14654695

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1uhm"

@@ Line 3: / Line 3: @@
 <StructureSection load='1uhm' size='340' side='right'caption='[[1uhm]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1uhm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UHM OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1UHM FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1uhm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UHM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UHM FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HHO1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HHO1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1uhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uhm OCA], [http://pdbe.org/1uhm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1uhm RCSB], [http://www.ebi.ac.uk/pdbsum/1uhm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1uhm ProSAT], [http://www.topsan.org/Proteins/RSGI/1uhm TOPSAN]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1uhm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uhm OCA], [https://pdbe.org/1uhm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uhm RCSB], [https://www.ebi.ac.uk/pdbsum/1uhm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uhm ProSAT], [https://www.topsan.org/Proteins/RSGI/1uhm TOPSAN]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/H1_YEAST H1_YEAST]] Could act as an H1-type linker histone. Has been shown to bind DNA.<ref>PMID:8772381</ref> <ref>PMID:9046096</ref>
+[[https://www.uniprot.org/uniprot/H1_YEAST H1_YEAST]] Could act as an H1-type linker histone. Has been shown to bind DNA.<ref>PMID:8772381</ref> <ref>PMID:9046096</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1uhm

From Proteopedia

Revision as of 06:45, 2 March 2022

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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