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PDBsum entry 2w2u
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protein Protein-protein interface(s) links
Hydrolase/transport PDB id
2w2u

 

 

 

 

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Contents
Protein chains
75 a.a. *
11 a.a. *
Waters ×118
* Residue conservation analysis
PDB id:
2w2u
Name: Hydrolase/transport
Title: Structural insight into the interaction between archaeal escrt-iii and aaa-atpase
Structure: Hypothetical p60 katanin. Chain: a, b. Fragment: mit domain, residues 1-75. Synonym: saci1372, aaa family atpase. Engineered: yes. Conserved archaeal protein. Chain: c, d. Fragment: residues 182-195. Synonym: saci1373.
Source: Sulfolobus acidocaldarius. Organism_taxid: 2285. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008. Expression_system_variant: c41 ripl. Synthetic: yes. Organism_taxid: 2285
Resolution:
2.20Å     R-factor:   0.227     R-free:   0.268
Authors: T.Obita,R.Y.Samson,O.Perisic,S.M.Freund,S.D.Bell,R.L.Williams
Key ref:
R.Y.Samson et al. (2008). A role for the ESCRT system in cell division in archaea. Science, 322, 1710-1713. PubMed id: 19008417 DOI: 10.1126/science.1165322
Date:
04-Nov-08     Release date:   14-Jul-09    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q877H3  (Q877H3_9CREN) -  AAA family ATPase from Sulfolobus acidocaldarius
Seq:
Struc: 		374 a.a.
75 a.a.
Protein chains
Pfam   ArchSchema ?
Q4J924  (CDVB_SULAC) -  Cell division protein B from Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Seq:
Struc: 		261 a.a.
11 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1126/science.1165322 Science 322:1710-1713 (2008)
PubMed id: 19008417  
 
 
A role for the ESCRT system in cell division in archaea.
R.Y.Samson, T.Obita, S.M.Freund, R.L.Williams, S.D.Bell.
 
  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.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. Localization of (Top) Saci1372 (Vps4) and (bottom) Saci1373 (ESCRT-III). Representative images are shown. Images show the FM4-64X staining for membrane (red), DAPI staining for DNA (blue), antibody labeling of ESCRT-III or Vps4(green), and merged images. Scale bar, 1 µm. Additional images are shown in figs. S6 and S7 and movie S1. 		Figure 3.
Fig. 3. (A) Interactions between ESCRT-III proteins detected by yeast two-hybrid analyses. Yeast cells containing the indicated plasmids were plated in media lacking leucine and tryptophan to select for plasmids and lacking histidine to score for interactions. (B) Identification of the minimal interaction site on Saci1373 (ESCRT-III) for binding Vps4. Glutathione S-transferase (GST) fusions of ESCRT-III fragments were used in pull-down assays with the full-length Vps4. The results of the pull-downs are shown in the lower panel. The input lanes contain 25 and 5% of input. (C) Identification of the interaction domain of Vps4 that binds Saci1373 (ESCRT-III). GST-Saci1373 (ESCRT-III) was used in pull-down assays with the full-length (1), C-terminal AAA+ domain (2), or isolated MIT domain (3) of Vps4. (D) A schematic representation of the interaction of Saci1373 (red) with the Saci1372 Vps4 MIT domain (yellow). (E) An illustration of the interaction of the yeast Vps4 MIT domain (yellow) with the C-terminal MIM1 motif (blue) of the yeast Vps2 ESCRT-III subunit. The MIM1 motif slots between MIT helices 2 and 3 (14). (F) The Saci1373 MIM2 (red)/Saci1372 MIT (yellow) interaction is closely related in structure with the CHMP6 MIM2 (green, extended)/VPS4A MIT (gray helices) interaction (20).
 
  The above figures are reprinted by permission from the AAAs: Science (2008, 322, 1710-1713) copyright 2008.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
22193162 T.E.Rusten, T.Vaccari, and H.Stenmark (2012).
Shaping development with ESCRTs.
  Nat Cell Biol, 14, 38-45.  
21113132 I.G.Duggin, N.Dubarry, and S.D.Bell (2011).
Replication termination and chromosome dimer resolution in the archaeon Sulfolobus solfataricus.
  EMBO J, 30, 145-153.  
21265756 J.C.Snyder, and M.J.Young (2011).
Potential role of cellular ESCRT proteins in the STIV life cycle.
  Biochem Soc Trans, 39, 107-110.  
21383202 N.Elia, R.Sougrat, T.A.Spurlin, J.H.Hurley, and J.Lippincott-Schwartz (2011).
Dynamics of endosomal sorting complex required for transport (ESCRT) machinery during cytokinesis and its role in abscission.
  Proc Natl Acad Sci U S A, 108, 4846-4851.  
21364937 P.C.Blainey, A.C.Mosier, A.Potanina, C.A.Francis, and S.R.Quake (2011).
Genome of a low-salinity ammonia-oxidizing archaeon determined by single-cell and metagenomic analysis.
  PLoS One, 6, e16626.  
21030261 S.Peel, P.Macheboeuf, N.Martinelli, and W.Weissenhorn (2011).
Divergent pathways lead to ESCRT-III-catalyzed membrane fission.
  Trends Biochem Sci, 36, 199-210.  
21572458 S.V.Albers, and B.H.Meyer (2011).
The archaeal cell envelope.
  Nat Rev Microbiol, 9, 414-426.  
  20671907 A.F.Ellen, B.Zolghadr, A.M.Driessen, and S.V.Albers (2010).
Shaping the archaeal cell envelope.
  Archaea, 2010, 608243.  
20598889 A.Spang, R.Hatzenpichler, C.Brochier-Armanet, T.Rattei, P.Tischler, E.Spieck, W.Streit, D.A.Stahl, M.Wagner, and C.Schleper (2010).
Distinct gene set in two different lineages of ammonia-oxidizing archaea supports the phylum Thaumarchaeota.
  Trends Microbiol, 18, 331-340.  
20421470 C.B.Walker, J.R.de la Torre, M.G.Klotz, H.Urakawa, N.Pinel, D.J.Arp, C.Brochier-Armanet, P.S.Chain, P.P.Chan, A.Gollabgir, J.Hemp, M.Hügler, E.A.Karr, M.Könneke, M.Shin, T.J.Lawton, T.Lowe, W.Martens-Habbena, L.A.Sayavedra-Soto, D.Lang, S.M.Sievert, A.C.Rosenzweig, G.Manning, and D.A.Stahl (2010).
Nitrosopumilus maritimus genome reveals unique mechanisms for nitrification and autotrophy in globally distributed marine crenarchaea.
  Proc Natl Acad Sci U S A, 107, 8818-8823.  
21115849 E.M.Coonrod, and T.H.Stevens (2010).
The yeast vps class E mutants: the beginning of the molecular genetic analysis of multivesicular body biogenesis.
  Mol Biol Cell, 21, 4057-4060.  
20616062 E.Morita, L.A.Colf, M.A.Karren, V.Sandrin, C.K.Rodesch, and W.I.Sundquist (2010).
Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance.
  Proc Natl Acad Sci U S A, 107, 12889-12894.  
20979330 H.P.Erickson, and M.Osawa (2010).
Cell division without FtsZ--a variety of redundant mechanisms.
  Mol Microbiol, 78, 267-270.  
20588296 J.H.Hurley, and P.I.Hanson (2010).
Membrane budding and scission by the ESCRT machinery: it's all in the neck.
  Nat Rev Mol Cell Biol, 11, 556-566.  
  20653365 J.H.Hurley (2010).
The ESCRT complexes.
  Crit Rev Biochem Mol Biol, 45, 463-487.  
21145455 J.H.Hurley, E.Boura, L.A.Carlson, and B.Różycki (2010).
Membrane budding.
  Cell, 143, 875-887.  
20459678 K.S.Makarova, and E.V.Koonin (2010).
Two new families of the FtsZ-tubulin protein superfamily implicated in membrane remodeling in diverse bacteria and archaea.
  Biol Direct, 5, 33.  
20818414 K.S.Makarova, N.Yutin, S.D.Bell, and E.V.Koonin (2010).
Evolution of diverse cell division and vesicle formation systems in Archaea.
  Nat Rev Microbiol, 8, 731-741.  
20949036 N.Neumann, D.Lundin, and A.M.Poole (2010).
Comparative genomic evidence for a complete nuclear pore complex in the last eukaryotic common ancestor.
  PLoS One, 5, e13241.  
21050804 R.Bernander, and T.J.Ettema (2010).
FtsZ-less cell division in archaea and bacteria.
  Curr Opin Microbiol, 13, 747-752.  
21079244 R.N.Bastos, and F.A.Barr (2010).
Plk1 negatively regulates Cep55 recruitment to the midbody to ensure orderly abscission.
  J Cell Biol, 191, 751-760.  
20221889 S.Berkner, A.Wlodkowski, S.V.Albers, and G.Lipps (2010).
Inducible and constitutive promoters for genetic systems in Sulfolobus acidocaldarius.
  Extremophiles, 14, 249-259.  
20844558 S.Gribaldo, A.M.Poole, V.Daubin, P.Forterre, and C.Brochier-Armanet (2010).
The origin of eukaryotes and their relationship with the Archaea: are we at a phylogenomic impasse?
  Nat Rev Microbiol, 8, 743-752.  
19535732 B.McDonald, and J.Martin-Serrano (2009).
No strings attached: the ESCRT machinery in viral budding and cytokinesis.
  J Cell Sci, 122, 2167-2177.  
19325624 C.Raiborg, and H.Stenmark (2009).
The ESCRT machinery in endosomal sorting of ubiquitylated membrane proteins.
  Nature, 458, 445-452.  
19680248 D.W.Adams, and J.Errington (2009).
Bacterial cell division: assembly, maintenance and disassembly of the Z ring.
  Nat Rev Microbiol, 7, 642-653.  
19477918 J.Xiao, X.W.Chen, B.A.Davies, A.R.Saltiel, D.J.Katzmann, and Z.Xu (2009).
Structural basis of Ist1 function and Ist1-Did2 interaction in the multivesicular body pathway and cytokinesis.
  Mol Biol Cell, 20, 3514-3524.
PDB codes: 3ggy 3ggz
19525971 M.Bajorek, H.L.Schubert, J.McCullough, C.Langelier, D.M.Eckert, W.M.Stubblefield, N.T.Uter, D.G.Myszka, C.P.Hill, and W.I.Sundquist (2009).
Structural basis for ESCRT-III protein autoinhibition.
  Nat Struct Mol Biol, 16, 754-762.
PDB codes: 3frr 3frs 3frt 3frv
19201590 M.C.Field, and J.B.Dacks (2009).
First and last ancestors: reconstructing evolution of the endomembrane system with ESCRTs, vesicle coat proteins, and nuclear pore complexes.
  Curr Opin Cell Biol, 21, 4.  
19527882 P.D.Bieniasz (2009).
The cell biology of HIV-1 virion genesis.
  Cell Host Microbe, 5, 550-558.  
19560911 P.I.Hanson, S.Shim, and S.A.Merrill (2009).
Cell biology of the ESCRT machinery.
  Curr Opin Cell Biol, 21, 568-574.  
19466751 P.L.Graumann (2009).
Dynamics of bacterial cytoskeletal elements.
  Cell Motil Cytoskeleton, 66, 909-914.  
19725809 P.Weiss, S.Huppert, and R.Kölling (2009).
Analysis of the dual function of the ESCRT-III protein Snf7 in endocytic trafficking and in gene expression.
  Biochem J, 424, 89-97.  
19783442 R.Y.Samson, and S.D.Bell (2009).
Ancient ESCRTs and the evolution of binary fission.
  Trends Microbiol, 17, 507-513.  
  19704896 T.J.Ettema, and R.Bernander (2009).
Cell division and the ESCRT complex: A surprise from the archaea.
  Commun Integr Biol, 2, 86-88.  
19331687 T.M.Venancio, S.Balaji, L.M.Iyer, and L.Aravind (2009).
Reconstructing the ubiquitin network - cross-talk with other systems and identification of novel functions.
  Genome Biol, 10, R33.  
19234443 T.Wollert, C.Wunder, J.Lippincott-Schwartz, and J.H.Hurley (2009).
Membrane scission by the ESCRT-III complex.
  Nature, 458, 172-177.  
19535731 T.Wollert, D.Yang, X.Ren, H.H.Lee, Y.J.Im, and J.H.Hurley (2009).
The ESCRT machinery at a glance.
  J Cell Sci, 122, 2163-2166.  
19492355 Y.Davidov, and E.Jurkevitch (2009).
Predation between prokaryotes and the origin of eukaryotes.
  Bioessays, 31, 748-757.  
19091952 J.M.Archibald (2008).
The eocyte hypothesis and the origin of eukaryotic cells.
  Proc Natl Acad Sci U S A, 105, 20049-20050.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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