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4zn3
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure of MjSpt4:Spt5 complex conformation B== | |
| + | <StructureSection load='4zn3' size='340' side='right' caption='[[4zn3]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4zn3]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZN3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZN3 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4zn1|4zn1]]</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=4zn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zn3 OCA], [http://pdbe.org/4zn3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zn3 RCSB], [http://www.ebi.ac.uk/pdbsum/4zn3 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/SPT5_METJA SPT5_METJA]] Stimulates transcription elongation.[HAMAP-Rule:MF_00950]<ref>PMID:20197319</ref> [[http://www.uniprot.org/uniprot/SPT4_METJA SPT4_METJA]] Stimulates transcription elongation.[HAMAP-Rule:MF_00949]<ref>PMID:20197319</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Spt5 (NusG in bacteria) is the only RNA polymerase-associated factor known to be conserved in all three domains of life. In archaea and eukaryotes, Spt5 associates with Spt4, an elongation factor that is absent in bacteria, to form a functional heterodimeric complex. Previous studies suggest that the Spt4:Spt5 complex interacts directly with DNA at the double-stranded DNA exit tunnel of RNA polymerase to regulate gene transcription. In this study, the DNA-binding ability of Spt4:Spt5 from the archaeon Methanocaldococcus jannaschii was confirmed via nuclear magnetic resonance chemical shift perturbation and fluorescence polarization assays. Crystallographic analysis of the full-length MjSpt4:Spt5 revealed two distinct conformations of the C-terminal KOW domain of Spt5. A similar alkaline region was found on the Spt4:Spt5 surface in both crystal forms, and identified as double-stranded DNA binding patch through mutagenesis-fluorescence polarization assays. Based on these structural and biochemical data, the Spt4:Spt5-DNA binding model was built for the first time. | ||
| - | + | Structural and biochemical insights into the DNA-binding mode of MjSpt4p:Spt5 complex at the exit tunnel of RNAPII.,Guo G, Gao Y, Zhu Z, Zhao D, Liu Z, Zhou H, Niu L, Teng M J Struct Biol. 2015 Dec;192(3):418-25. doi: 10.1016/j.jsb.2015.09.023. Epub 2015 , Oct 14. PMID:26433031<ref>PMID:26433031</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 4zn3" style="background-color:#fffaf0;"></div> |
| - | [[Category: Guo, G | + | == References == |
| - | [[Category: Niu, L | + | <references/> |
| - | [[Category: Teng, M | + | __TOC__ |
| - | [[Category: Zhou, H | + | </StructureSection> |
| - | [[Category: | + | [[Category: Gao, Y X]] |
| + | [[Category: Guo, G R]] | ||
| + | [[Category: Niu, L W]] | ||
| + | [[Category: Teng, M K]] | ||
| + | [[Category: Zhou, H H]] | ||
| + | [[Category: Zhu, Z L]] | ||
| + | [[Category: Protein-protein complex]] | ||
| + | [[Category: Transcription]] | ||
Revision as of 03:46, 11 May 2016
Crystal Structure of MjSpt4:Spt5 complex conformation B
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