2W2U
STRUCTURAL INSIGHT INTO THE INTERACTION BETWEEN ARCHAEAL ESCRT-III AND AAA-ATPASE
Summary for 2W2U
| Entry DOI | 10.2210/pdb2w2u/pdb |
| Related | 2V6Y |
| Descriptor | HYPOTHETICAL P60 KATANIN, CONSERVED ARCHAEAL PROTEIN (3 entities in total) |
| Functional Keywords | hydrolase transport complex, nucleotide-binding, escrt, aaa-atpase, cytokinesis, atp-binding, hydrolase-transport complex, hydrolase/transport |
| Biological source | SULFOLOBUS ACIDOCALDARIUS More |
| Cellular location | Cytoplasm, nucleoid : Q4J924 |
| Total number of polymer chains | 4 |
| Total formula weight | 22451.82 |
| Authors | Obita, T.,Samson, R.Y.,Perisic, O.,Freund, S.M.,Bell, S.D.,Williams, R.L. (deposition date: 2008-11-04, release date: 2009-07-14, Last modification date: 2023-12-13) |
| Primary citation | Samson, R.Y.,Obita, T.,Freund, S.M.,Williams, R.L.,Bell, S.D. A Role for the Escrt System in Cell Division in Archaea. Science, 322:1710-, 2008 Cited by PubMed Abstract: Archaea are prokaryotic organisms that lack endomembrane structures. However, a number of hyperthermophilic members of the Kingdom Crenarchaea, including members of the Sulfolobus genus, encode homologs of the eukaryotic endosomal sorting system components Vps4 and ESCRT-III (endosomal sorting complex required for transport-III). We found that Sulfolobus ESCRT-III and Vps4 homologs underwent regulation of their expression during the cell cycle. The proteins interacted and we established the structural basis of this interaction. Furthermore, these proteins specifically localized to the mid-cell during cell division. Overexpression of a catalytically inactive mutant Vps4 in Sulfolobus resulted in the accumulation of enlarged cells, indicative of failed cell division. Thus, the archaeal ESCRT system plays a key role in cell division. PubMed: 19008417DOI: 10.1126/SCIENCE.1165322 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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