5L3X

Crystal structure of negative elongation factor subcomplex NELF-AC

Summary for 5L3X

• Entry DOI: 10.2210/pdb5l3x/pdb
• Descriptor: Negative elongation factor A, Negative elongation factor C/D, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: transcription, repressor, transcription regulation, gene expression
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus : Q9H3P2 Q8IXH7
• Total number of polymer chains: 2
• Total formula weight: 65043.94

Authors

Poellmann, D.,Vos, S.M.,Cramer, P. (deposition date: 2016-05-24, release date: 2016-06-22, Last modification date: 2024-05-08)

Primary citation

Vos, S.M.,Pollmann, D.,Caizzi, L.,Hofmann, K.B.,Rombaut, P.,Zimniak, T.,Herzog, F.,Cramer, P.
Architecture and RNA binding of the human negative elongation factor.
Elife, 5:-, 2016

PubMed Abstract: Transcription regulation in metazoans often involves promoter-proximal pausing of RNA polymerase (Pol) II, which requires the 4-subunit negative elongation factor (NELF). Here we discern the functional architecture of human NELF through X-ray crystallography, protein crosslinking, biochemical assays, and RNA crosslinking in cells. We identify a NELF core subcomplex formed by conserved regions in subunits NELF-A and NELF-C, and resolve its crystal structure. The NELF-AC subcomplex binds single-stranded nucleic acids in vitro, and NELF-C associates with RNA in vivo. A positively charged face of NELF-AC is involved in RNA binding, whereas the opposite face of the NELF-AC subcomplex binds NELF-B. NELF-B is predicted to form a HEAT repeat fold, also binds RNA in vivo, and anchors the subunit NELF-E, which is confirmed to bind RNA in vivo. These results reveal the three-dimensional architecture and three RNA-binding faces of NELF.

PubMed: 27282391
DOI: 10.7554/eLife.14981

Experimental method

X-RAY DIFFRACTION (2.75 Å)