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-Structure paper
Title | Structural studies of a bacterial condensin complex reveal ATP-dependent disruption of intersubunit interactions. |
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Journal, issue, pages | Cell(Cambridge,Mass. ), Vol. 136, Page 85-96, Year 2009 |
Publish date | Oct 10, 2008 (structure data deposition date) |
![]() | Woo, J.S. / Lim, J.H. / Shin, H.C. / Suh, M.K. / Ku, B. / Lee, K.H. / Joo, K. / Robinson, H. / Lee, J. / Park, S.Y. ...Woo, J.S. / Lim, J.H. / Shin, H.C. / Suh, M.K. / Ku, B. / Lee, K.H. / Joo, K. / Robinson, H. / Lee, J. / Park, S.Y. / Ha, N.C. / Oh, B.H. |
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Methods | X-ray diffraction |
Resolution | 2.9 - 4 Å |
Structure data | ![]() PDB-3euh: ![]() PDB-3euj: ![]() PDB-3euk: |
Chemicals | ![]() ChemComp-GLY: ![]() ChemComp-HOH: ![]() ChemComp-AGS: ![]() ChemComp-MG: |
Source |
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![]() | CELL CYCLE / Chromosome condensation / condensin / non-SMC subunit / kleisin / MukE / MukF / Calcium / Cell division / Chromosome partition / Cytoplasm / DNA condensation / MukB / SMC / ABC-type ATPase / WHD / ATP-binding / DNA-binding / Nucleotide-binding |