|
|
| Line 3: |
Line 3: |
| | <StructureSection load='4nq0' size='340' side='right'caption='[[4nq0]], [[Resolution|resolution]] 2.10Å' scene=''> | | <StructureSection load='4nq0' size='340' side='right'caption='[[4nq0]], [[Resolution|resolution]] 2.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4nq0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NQ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NQ0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4nq0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NQ0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NQ0 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HIF1, YLL022C, L1205 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | + | </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=4nq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nq0 OCA], [https://pdbe.org/4nq0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nq0 RCSB], [https://www.ebi.ac.uk/pdbsum/4nq0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nq0 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4nq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nq0 OCA], [http://pdbe.org/4nq0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nq0 RCSB], [http://www.ebi.ac.uk/pdbsum/4nq0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nq0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/HIF1_YEAST HIF1_YEAST]] Histone H3 and H4 specific chaperone component of the nuclear histone acetyltransferase B (HAT-B) complex. Involved in chromatin assembly and telomere silencing.<ref>PMID:14761951</ref> <ref>PMID:15099519</ref> | + | [https://www.uniprot.org/uniprot/HIF1_YEAST HIF1_YEAST] Histone H3 and H4 specific chaperone component of the nuclear histone acetyltransferase B (HAT-B) complex. Involved in chromatin assembly and telomere silencing.<ref>PMID:14761951</ref> <ref>PMID:15099519</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 22: |
Line 21: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Gao, Y]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: He, W]] | + | [[Category: Gao Y]] |
| - | [[Category: Liu, H]] | + | [[Category: He W]] |
| - | [[Category: Niu, L]] | + | [[Category: Liu H]] |
| - | [[Category: Teng, M]] | + | [[Category: Niu L]] |
| - | [[Category: Zhang, M]] | + | [[Category: Teng M]] |
| - | [[Category: Zhu, Z]] | + | [[Category: Zhang M]] |
| - | [[Category: Chaperone]]
| + | [[Category: Zhu Z]] |
| - | [[Category: Histone chaperone]]
| + | |
| - | [[Category: Mediating protein-protein interaction]]
| + | |
| - | [[Category: Nasp homologue]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Shni-tpr]]
| + | |
| - | [[Category: Tpr]]
| + | |
| Structural highlights
Function
HIF1_YEAST Histone H3 and H4 specific chaperone component of the nuclear histone acetyltransferase B (HAT-B) complex. Involved in chromatin assembly and telomere silencing.[1] [2]
Publication Abstract from PubMed
Yeast Hif1, a homologue of human nuclear autoantigenic sperm protein (NASP), is a histone chaperone that involved in various protein complexes modifying histones during telomeric silencing and chromatin reassembly. For elucidating the structural basis of Hif1, here, we present crystal structure of Hif1 that consists of a superhelixed TPR domain and an extended acid loop covering the rear of TPR domain, which represents typical characters of SHNi-TPR (Sim3-Hif1-NASP interrupted TPR) proteins. Our binding assay indicates that Hif1 could bind to histone octamer via histone H3 and H4. However, the acid loop is crucial for the binding of histones while it may also change the conformation of TPR groove. By binding to core histone complex Hif1 may recruit functional protein complexes to modify histones during chromatin reassembly.
Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones.,Liu H, Zhang M, He W, Zhu Z, Teng M, Gao Y, Niu L Biochem J. 2014 Jun 20. PMID:24946827[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Poveda A, Pamblanco M, Tafrov S, Tordera V, Sternglanz R, Sendra R. Hif1 is a component of yeast histone acetyltransferase B, a complex mainly localized in the nucleus. J Biol Chem. 2004 Apr 16;279(16):16033-43. Epub 2004 Feb 3. PMID:14761951 doi:http://dx.doi.org/10.1074/jbc.M314228200
- ↑ Ai X, Parthun MR. The nuclear Hat1p/Hat2p complex: a molecular link between type B histone acetyltransferases and chromatin assembly. Mol Cell. 2004 Apr 23;14(2):195-205. PMID:15099519
- ↑ Liu H, Zhang M, He W, Zhu Z, Teng M, Gao Y, Niu L. Structural insights into yeast histone chaperone Hif1: a scaffold protein recruiting protein complexes to core histones. Biochem J. 2014 Jun 20. PMID:24946827 doi:http://dx.doi.org/10.1042/BJ20131640
|
