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PDBsum entry 3eab
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protein Protein-protein interface(s) links
Cell cycle PDB id
3eab

 

 

 

 

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Contents
Protein chains
(+ 0 more) 89 a.a. *
40 a.a. *
39 a.a. *
41 a.a. *
37 a.a. *
38 a.a. *
37 a.a. *
* Residue conservation analysis
PDB id:
3eab
Name: Cell cycle
Title: Crystal structure of spastin mit in complex with escrt iii
Structure: Spastin. Chain: a, b, c, d, e, f. Fragment: unp residues 112 to 196. Engineered: yes. Chmp1b. Chain: g, h, i, j, k, l. Fragment: unp residues 145 to 194. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: spast, kiaa1083, spg4. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_taxid: 562
Resolution:
2.50Å     R-factor:   0.232     R-free:   0.268
Authors: D.Yang,N.Rimanchi,B.Renvoise,J.Lippincott-Schwartz,C.Blackstone, J.H.Hurley
Key ref:
D.Yang et al. (2008). Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B. Nat Struct Biol, 15, 1278-1286. PubMed id: 18997780 DOI: 10.1038/nsmb.1512
Date:
25-Aug-08     Release date:   11-Nov-08    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9UBP0  (SPAST_HUMAN) -  Spastin from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		616 a.a.
89 a.a.*
Protein chain
Pfam   ArchSchema ?
Q7LBR1  (CHM1B_HUMAN) -  Charged multivesicular body protein 1b from Homo sapiens
Seq:
Struc: 		199 a.a.
40 a.a.
Protein chain
Pfam   ArchSchema ?
Q7LBR1  (CHM1B_HUMAN) -  Charged multivesicular body protein 1b from Homo sapiens
Seq:
Struc: 		199 a.a.
39 a.a.
Protein chain
Pfam   ArchSchema ?
Q7LBR1  (CHM1B_HUMAN) -  Charged multivesicular body protein 1b from Homo sapiens
Seq:
Struc: 		199 a.a.
41 a.a.
Protein chain
Pfam   ArchSchema ?
Q7LBR1  (CHM1B_HUMAN) -  Charged multivesicular body protein 1b from Homo sapiens
Seq:
Struc: 		199 a.a.
37 a.a.
Protein chain
Pfam   ArchSchema ?
Q7LBR1  (CHM1B_HUMAN) -  Charged multivesicular body protein 1b from Homo sapiens
Seq:
Struc: 		199 a.a.
38 a.a.
Protein chain
Pfam   ArchSchema ?
Q7LBR1  (CHM1B_HUMAN) -  Charged multivesicular body protein 1b from Homo sapiens
Seq:
Struc: 		199 a.a.
37 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 4 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class 2: Chains A, B, C, D, E, F: E.C.5.6.1.1  - microtubule-severing ATPase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: n ATP + n H2O + a microtubule = n ADP + n phosphate + (n+1) alpha/beta tubulin heterodimers
n ATP
 + n H2O
 + microtubule
 = n ADP
 + n phosphate
 + (n+1) alpha/beta tubulin heterodimers
   Enzyme class 3: Chains G, H, I, J, K, L: E.C.?
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1038/nsmb.1512 Nat Struct Biol 15:1278-1286 (2008)
PubMed id: 18997780  
 
 
Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B.
D.Yang, N.Rismanchi, B.Renvoisé, J.Lippincott-Schwartz, C.Blackstone, J.H.Hurley.
 
  ABSTRACT  
 
The endosomal sorting complex required for transport (ESCRT) machinery, including ESCRT-III, localizes to the midbody and participates in the membrane-abscission step of cytokinesis. The ESCRT-III protein charged multivesicular body protein 1B (CHMP1B) is required for recruitment of the MIT domain-containing protein spastin, a microtubule-severing enzyme, to the midbody. The 2.5-A structure of the C-terminal tail of CHMP1B with the MIT domain of spastin reveals a specific, high-affinity complex involving a noncanonical binding site between the first and third helices of the MIT domain. The structural interface is twice as large as that of the MIT domain of the VPS4-CHMP complex, consistent with the high affinity of the interaction. A series of unique hydrogen-bonding interactions and close packing of small side chains discriminate against the other ten human ESCRT-III subunits. Point mutants in the CHMP1B binding site of spastin block recruitment of spastin to the midbody and impair cytokinesis.
 
  Selected figure(s)  
 
Figure 3.
(a) Overall structure of the MIT domain (blue) and CHMP1B (orange). (b) Key MIM leucine residues bind to hydrophobic pockets in the groove between 1 and 3 of the MIT domain. The spastin MIT domain surface is colored green for carbon atoms, red for oxygen and blue for nitrogen. Contiguous green regions indicate hydrophobic surfaces. (c) Overview of polar interactions between CHMP1B-CTR and the spastin MIT domain. (d–f) Details of interactions as seen in insets d–f within c. 		Figure 5.
(a) HeLa cells expressing wild-type (WT) Myc-spastin (above, green) or Myc–spastin-H120D F124D (below, green) were co-immunostained for Myc epitope and -tubulin.
 
  The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: Nat Struct Biol (2008, 15, 1278-1286) copyright 2008.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
22552143 J.P.Fededa, and D.W.Gerlich (2012).
Molecular control of animal cell cytokinesis.
  Nat Cell Biol, 14, 440-447.  
21436431 C.Raiborg, and H.Stenmark (2011).
Cell biology. A helix for the final cut.
  Science, 331, 1533-1534.  
21310966 J.Guizetti, L.Schermelleh, J.Mäntler, S.Maar, I.Poser, H.Leonhardt, T.Müller-Reichert, and D.W.Gerlich (2011).
Cortical constriction during abscission involves helices of ESCRT-III-dependent filaments.
  Science, 331, 1616-1620.  
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.  
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.  
20362686 A.Hervás-Aguilar, O.Rodríguez-Galán, A.Galindo, J.F.Abenza, H.N.Arst, and M.A.Peñalva (2010).
Characterization of Aspergillus nidulans DidB Did2, a non-essential component of the multivesicular body pathway.
  Fungal Genet Biol, 47, 636-646.  
20208530 A.P.Sagona, I.P.Nezis, N.M.Pedersen, K.Liestøl, J.Poulton, T.E.Rusten, R.I.Skotheim, C.Raiborg, and H.Stenmark (2010).
PtdIns(3)P controls cytokinesis through KIF13A-mediated recruitment of FYVE-CENT to the midbody.
  Nat Cell Biol, 12, 362-371.  
19963362 A.Roll-Mecak, and F.J.McNally (2010).
Microtubule-severing enzymes.
  Curr Opin Cell Biol, 22, 96.  
20719964 B.Renvoisé, R.L.Parker, D.Yang, J.C.Bakowska, J.H.Hurley, and C.Blackstone (2010).
SPG20 protein spartin is recruited to midbodies by ESCRT-III protein Ist1 and participates in cytokinesis.
  Mol Biol Cell, 21, 3293-3303.  
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.  
20222872 I.Roxrud, H.Stenmark, and L.Malerød (2010).
ESCRT & Co.
  Biol Cell, 102, 293-318.  
20708087 J.Guizetti, and D.W.Gerlich (2010).
Cytokinetic abscission in animal cells.
  Semin Cell Dev Biol, 21, 909-916.  
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.  
20430936 J.M.Solowska, J.Y.Garbern, and P.W.Baas (2010).
Evaluation of loss of function as an explanation for SPG4-based hereditary spastic paraplegia.
  Hum Mol Genet, 19, 2767-2779.  
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.  
20186698 P.Przybylski, K.Pyta, J.Stefańska, B.Brzezinski, and F.Bartl (2010).
Structure elucidation, complete NMR assignment and PM5 theoretical studies of new hydroxy-aminoalkyl-alpha,beta-unsaturated derivatives of the macrolide antibiotic josamycin.
  Magn Reson Chem, 48, 286-296.  
20017116 R.L.Rich, and D.G.Myszka (2010).
Grading the commercial optical biosensor literature-Class of 2008: 'The Mighty Binders'.
  J Mol Recognit, 23, 1.  
20200447 S.H.Park, P.P.Zhu, R.L.Parker, and C.Blackstone (2010).
Hereditary spastic paraplegia proteins REEP1, spastin, and atlastin-1 coordinate microtubule interactions with the tubular ER network.
  J Clin Invest, 120, 1097-1110.  
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.  
19277045 G.W.Gould, and J.Lippincott-Schwartz (2009).
New roles for endosomes: from vesicular carriers to multi-purpose platforms.
  Nat Rev Mol Cell Biol, 10, 287-292.  
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
19823194 P.A.Dion, H.Daoud, and G.A.Rouleau (2009).
Genetics of motor neuron disorders: new insights into pathogenic mechanisms.
  Nat Rev Genet, 10, 769-782.  
19733077 P.Steigemann, and D.W.Gerlich (2009).
Cytokinetic abscission: cellular dynamics at the midbody.
  Trends Cell Biol, 19, 606-616.  
19783442 R.Y.Samson, and S.D.Bell (2009).
Ancient ESCRTs and the evolution of binary fission.
  Trends Microbiol, 17, 507-513.  
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.  
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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