4M8B

Fungal Protein

4M8B の概要

• エントリーDOI: 10.2210/pdb4m8b/pdb
• 分子名称: Chain A of dsDNA containing the cis-regulatory element, Chain B of dsDNA containing the cis-regulatory element, YHR177W, ... (5 entities in total)
• 機能のキーワード: wopr fungal-pathogenesis transcription, wopr domain, transcription factor, transcription, transcription-dna complex, transcription/dna
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 35736.33

構造登録者

Rosenberg, O.S.,Lohse, M.L.,Stroud, R.M.,Johnson, A.D. (登録日: 2013-08-13, 公開日: 2014-06-25, 最終更新日: 2024-04-03)

主引用文献

Lohse, M.B.,Rosenberg, O.S.,Cox, J.S.,Stroud, R.M.,Finer-Moore, J.S.,Johnson, A.D.
Structure of a new DNA-binding domain which regulates pathogenesis in a wide variety of fungi.
Proc.Natl.Acad.Sci.USA, 111:10404-10410, 2014

PubMed Abstract: WOPR-domain proteins are found throughout the fungal kingdom where they function as master regulators of cell morphology and pathogenesis. Genetic and biochemical experiments previously demonstrated that these proteins bind to specific DNA sequences and thereby regulate transcription. However, their primary sequence showed no relationship to any known DNA-binding domain, and the basis for their ability to recognize DNA sequences remained unknown. Here, we describe the 2.6-Å crystal structure of a WOPR domain in complex with its preferred DNA sequence. The structure reveals that two highly conserved regions, separated by an unconserved linker, form an interdigitated β-sheet that is tilted into the major groove of DNA. Although the main interaction surface is in the major groove, the highest-affinity interactions occur in the minor groove, primarily through a deeply penetrating arginine residue. The structure reveals a new, unanticipated mechanism by which proteins can recognize specific sequences of DNA.

PubMed: 24994900
DOI: 10.1073/pnas.1410110111

実験手法

X-RAY DIFFRACTION (2.61 Å)