2NS2

Crystal Structure of Spindlin1

Summary for 2NS2

• Entry DOI: 10.2210/pdb2ns2/pdb
• Descriptor: Spindlin-1, PHOSPHATE ION (3 entities in total)
• Functional Keywords: beta barrel, repeat domains, cell cycle
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: Q9Y657
• Total number of polymer chains: 2
• Total formula weight: 55244.44

Authors

Zhao, Q.,Qin, L.,Jiang, F.,Wu, B.,Yue, W.,Xu, F.,Rong, Z.,Yuan, H.,Xie, X.,Gao, Y.,Bai, C.,Bartlam, M. (deposition date: 2006-11-02, release date: 2006-11-28, Last modification date: 2023-12-27)

Primary citation

Zhao, Q.,Qin, L.,Jiang, F.,Wu, B.,Yue, W.,Xu, F.,Rong, Z.,Yuan, H.,Xie, X.,Gao, Y.,Bai, C.,Bartlam, M.,Pei, X.,Rao, Z.
Structure of human spindlin1. Tandem tudor-like domains for cell cycle regulation
J.Biol.Chem., 282:647-656, 2007

PubMed Abstract: Spindlin1, a meiotic spindle-binding protein that is highly expressed in ovarian cancer cells, was first identified as a gene involved in gametogenesis. It appeared to be a target for cell cycle-dependent phosphorylation and was demonstrated to disturb the cell cycle. Here we report the crystal structure of human spindlin1 to 2.2A of resolution, representing the first three-dimensional structure from the spin/ssty (Y-linked spermiogenesis-specific transcript) gene family. The refined structure, containing three repeats of five/four anti-parallel beta-strands, exhibits a novel arrangement of tandem Tudor-like domains. Two phosphate ions, chelated by Thr-95 and other residues, appear to stabilize the long loop between domains I and II, which might mediate the cell cycle regulation activity of spindlin1. Flow cytometry experiments indicate that cells expressing spindlin1 display a different cell cycle distribution in mitosis, whereas those expressing a T95A mutant, which had a great decrease in phosphorous content, have little effect on the cell cycle. We further identified associations of spindlin1 with nucleic acid to provide a biochemical basis for its cell cycle regulation and other functions.

PubMed: 17082182
DOI: 10.1074/jbc.M604029200

Experimental method

X-RAY DIFFRACTION (2.2 Å)