Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3HTK

Crystal structure of Mms21 and Smc5 complex

Summary for 3HTK
Entry DOI10.2210/pdb3htk/pdb
DescriptorStructural maintenance of chromosomes protein 5, E3 SUMO-protein ligase MMS21, ZINC ION, ... (5 entities in total)
Functional Keywordssumo e3 ligase, spl-ring, ring, atp-binding, chromosomal protein, coiled coil, dna damage, dna recombination, dna repair, nucleotide-binding, nucleus, ubl conjugation, cytoplasm, ligase, metal-binding, ubl conjugation pathway, zinc, zinc-finger, recombination-replication-ligase complex, recombination/replication/ligase
Biological sourceSaccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
More
Cellular locationNucleus (Potential): Q08204 Q08204
Nucleus: P38632
Total number of polymer chains3
Total formula weight46198.82
Authors
Duan, X.,Sarangi, P.,Liu, X.,Rangi, G.K.,Zhao, X.,Ye, H. (deposition date: 2009-06-11, release date: 2009-10-20, Last modification date: 2024-02-21)
Primary citationDuan, X.,Sarangi, P.,Liu, X.,Rangi, G.K.,Zhao, X.,Ye, H.
Structural and functional insights into the roles of the Mms21 subunit of the Smc5/6 complex.
Mol.Cell, 35:657-668, 2009
Cited by
PubMed Abstract: The Smc5/6 complex is an evolutionarily conserved chromosomal ATPase required for cell growth and DNA repair. Its Mms21 subunit supports both functions by docking to the arm region of Smc5 and providing SUMO ligase activity. Here, we report the crystal structure of Mms21 in complex with the Smc5 arm. Our structure revealed two distinct structural and functional domains of the Smc5-bound Mms21: its N-terminal half is dedicated to Smc5 binding by forming a helix bundle with a coiled-coil structure of Smc5; its C-terminal half includes the SUMO ligase domain, which adopts a new type of RING E3 structure. Mutagenesis and structural analyses showed that the Mms21-Smc5 interface is required for cell growth and resistance to DNA damage, while the unique Mms21 RING domain confers specificity to the SUMO E2-E3 interaction. Through structure-based dissection of Mms21 functions, our studies establish a framework for understanding its roles in the Smc5/6 complex.
PubMed: 19748359
DOI: 10.1016/j.molcel.2009.06.032
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.31 Å)
Structure validation

237735

数据于2025-06-18公开中

PDB statisticsPDBj update infoContact PDBjnumon