1X4S

Solution structure of zinc finger HIT domain in protein FON

Summary for 1X4S

• Entry DOI: 10.2210/pdb1x4s/pdb
• NMR Information: BMRB: 11363
• Descriptor: Zinc finger HIT domain containing protein 2, ZINC ION (2 entities in total)
• Functional Keywords: zinc finger hit domain, structural genomics, nppsfa, national project on protein structural and functional analyses, riken structural genomics/proteomics initiative, rsgi, metal binding protein
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 6220.55

Authors

He, F.,Muto, Y.,Inoue, M.,Kigawa, T.,Shirouzu, M.,Terada, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2005-05-14, release date: 2005-11-14, Last modification date: 2024-05-29)

Primary citation

He, F.,Umehara, T.,Tsuda, K.,Inoue, M.,Kigawa, T.,Matsuda, T.,Yabuki, T.,Aoki, M.,Seki, E.,Terada, T.,Shirouzu, M.,Tanaka, A.,Sugano, S.,Muto, Y.,Yokoyama, S.
Solution structure of the zinc finger HIT domain in protein FON
Protein Sci., 16:1577-1587, 2007

PubMed Abstract: The zinc finger HIT domain is a sequence motif found in many proteins, including thyroid hormone receptor interacting protein 3 (TRIP-3), which is possibly involved in maturity-onset diabetes of the young (MODY). Novel zinc finger motifs are suggested to play important roles in gene regulation and chromatin remodeling. Here, we determined the high-resolution solution structure of the zinc finger HIT domain in ZNHIT2 (protein FON) from Homo sapiens, by an NMR method based on 567 upper distance limits derived from NOE intensities measured in three-dimensional NOESY spectra. The structure yielded a backbone RMSD to the mean coordinates of 0.19 A for the structured residues 12-48. The fold consists of two consecutive antiparallel beta-sheets and two short C-terminal helices packed against the second beta-sheet, and binds two zinc ions. Both zinc ions are coordinated tetrahedrally via a CCCC-CCHC motif to the ligand residues of the zf-HIT domain in an interleaved manner. The tertiary structure of the zinc finger HIT domain closely resembles the folds of the B-box, RING finger, and PHD domains with a cross-brace zinc coordination mode, but is distinct from them. The unique three-dimensional structure of the zinc finger HIT domain revealed a novel zinc-binding fold, as a new member of the treble clef domain family. On the basis of the structural data, we discuss the possible functional roles of the zinc finger HIT domain.

PubMed: 17656577
DOI: 10.1110/ps.062635107

Experimental method

SOLUTION NMR