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PDBsum entry 1w2e

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protein Protein-protein interface(s) links
Bacterial cell division PDB id
1w2e
Jmol
Contents
Protein chains
92 a.a. *
Waters ×12
* Residue conservation analysis
PDB id:
1w2e
Name: Bacterial cell division
Title: The crystal structure of the bacterial cell division protein zapa
Structure: Zapa. Chain: a, b. Synonym: hypothetical protein pa5227. Engineered: yes
Source: Pseudomonas aeruginosa. Organism_taxid: 287. Strain: pa01-lac. Atcc: 47085d. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Tetramer (from PDB file)
Resolution:
2.80Å     R-factor:   0.240     R-free:   0.288
Authors: H.H.Low,M.C.Moncrieffe,J.Lowe
Key ref:
H.H.Low et al. (2004). The crystal structure of ZapA and its modulation of FtsZ polymerisation. J Mol Biol, 341, 839-852. PubMed id: 15288790 DOI: 10.1016/j.jmb.2004.05.031
Date:
01-Jul-04     Release date:   19-Jul-04    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9HTW3  (ZAPA_PSEAE) -  Cell division protein ZapA
Seq:
Struc:
104 a.a.
92 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     cell cycle   3 terms 

 

 
DOI no: 10.1016/j.jmb.2004.05.031 J Mol Biol 341:839-852 (2004)
PubMed id: 15288790  
 
 
The crystal structure of ZapA and its modulation of FtsZ polymerisation.
H.H.Low, M.C.Moncrieffe, J.Löwe.
 
  ABSTRACT  
 
FtsZ is part of a mid-cell cytokinetic structure termed the Z-ring that recruits a hierarchy of fission related proteins early in the bacterial cell cycle. The widely conserved ZapA has been shown to interact with FtsZ, to drive its polymerisation and to promote FtsZ filament bundling thereby contributing to the spatio-temporal tuning of the Z-ring. Here, we show the crystal structure of ZapA (11.6 kDa) from Pseudomonas aeruginosa at 2.8 A resolution. The electron density reveals two dimers associating via an extensive C-terminal coiled-coil protrusion to form an elongated anti-parallel tetramer. In solution, ZapA exists in a dimer-tetramer equilibrium that is strongly correlated with concentration. An increase in concentration promotes formation of the higher oligomeric state. The dimer is postulated to be the predominant physiological species although the tetramer could become significant if, as FtsZ is integrated into the Z-ring and is cross-linked, the local concentration of the dimer becomes sufficiently high. We also show that ZapA binds FtsZ with an approximate 1:1 molar stoichiometry and that this interaction provokes dramatic FtsZ polymerisation and inter-filament association as well as yielding filaments, single or bundled, more stable and resistant to collapse. Whilst in vitro dynamics of FtsZ are well characterised, its in vivo arrangement within the ultra-structural architecture of the Z-ring is yet to be determined despite being fundamental to cell division. The ZapA dimer has single 2-fold symmetry whilst the bipolar tetramer displays triple 2-fold symmetry. Given the symmetry of these ZapA oligomers and the polar nature of FtsZ filaments, the structure of ZapA carries novel implications for the inherent architecture of the Z-ring in vivo.
 
  Selected figure(s)  
 
Figure 3.
Figure 3. Stereo image showing the conformation of the four H2 helices in a ZapA tetramer with their side-chains exposed. The tetramerisation domain is formed by extensive overlap between the C termini of the H2 helices. This region is characterised by a central hydrophobic core and surrounding hydrophilic amino acid residues with interdigitating side-chains. In contrast, the dimerisation domain is located towards the opposite ends of the H2 helices with inter-helix proximity and contact increasing towards the N termini.
Figure 6.
Figure 6. A, Surface map displaying the electrostatic potential of the ZapA dimer. Coloured from -6.0 kT/e, red to 6.0 kT/e, blue. Orientation is similar to subunits AB in Figure 2B. B, A grading of inter-species residue conservation from 25 ZapA sequences; a spectrum from red, highly conserved through to dark blue, least conserved. Orientation is similar to subunits AB in Figure 2B.
 
  The above figures are reprinted by permission from Elsevier: J Mol Biol (2004, 341, 839-852) copyright 2004.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21049125 V.N.Uversky (2011).
Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes.
  Chem Soc Rev, 40, 1623-1634.  
20969647 A.Dajkovic, S.Pichoff, J.Lutkenhaus, and D.Wirtz (2010).
Cross-linking FtsZ polymers into coherent Z rings.
  Mol Microbiol, 78, 651-668.  
20943430 P.A.de Boer (2010).
Advances in understanding E. coli cell fission.
  Curr Opin Microbiol, 13, 730-737.  
20629754 P.M.Martins, I.F.Lau, M.Bacci, J.Belasque, A.M.do Amaral, S.R.Taboga, and H.Ferreira (2010).
Subcellular localization of proteins labeled with GFP in Xanthomonas citri ssp. citri: targeting the division septum.
  FEMS Microbiol Lett, 310, 76-83.  
20497333 S.Alexeeva, T.W.Gadella, J.Verheul, G.S.Verhoeven, and T.den Blaauwen (2010).
Direct interactions of early and late assembling division proteins in Escherichia coli cells resolved by FRET.
  Mol Microbiol, 77, 384-398.  
  19849848 A.Paez, P.Mateos-Gil, I.Hörger, J.Mingorance, G.Rivas, M.Vicente, M.Vélez, and P.Tarazona (2009).
Simple modeling of FtsZ polymers on flat and curved surfaces: correlation with experimental in vitro observations.
  PMC Biophys, 2, 8.  
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.  
19842714 T.Mohammadi, G.E.Ploeger, J.Verheul, A.D.Comvalius, A.Martos, C.Alfonso, J.van Marle, G.Rivas, and T.den Blaauwen (2009).
The GTPase activity of Escherichia coli FtsZ determines the magnitude of the FtsZ polymer bundling by ZapA in vitro.
  Biochemistry, 48, 11056-11066.  
18291654 A.Dajkovic, G.Lan, S.X.Sun, D.Wirtz, and J.Lutkenhaus (2008).
MinC spatially controls bacterial cytokinesis by antagonizing the scaffolding function of FtsZ.
  Curr Biol, 18, 235-244.  
18312270 F.van den Ent, T.M.Vinkenvleugel, A.Ind, P.West, D.Veprintsev, N.Nanninga, T.den Blaauwen, and J.Löwe (2008).
Structural and mutational analysis of the cell division protein FtsQ.
  Mol Microbiol, 68, 110-123.
PDB codes: 2vh1 2vh2
18394147 G.Ebersbach, E.Galli, J.Møller-Jensen, J.Löwe, and K.Gerdes (2008).
Novel coiled-coil cell division factor ZapB stimulates Z ring assembly and cell division.
  Mol Microbiol, 68, 720-735.
PDB code: 2jee
18782755 J.K.Singh, R.D.Makde, V.Kumar, and D.Panda (2008).
SepF Increases the Assembly and Bundling of FtsZ Polymers and Stabilizes FtsZ Protofilaments by Binding along Its Length.
  J Biol Chem, 283, 31116-31124.  
18323848 R.L.Lock, and E.J.Harry (2008).
Cell-division inhibitors: new insights for future antibiotics.
  Nat Rev Drug Discov, 7, 324-338.  
18291013 T.den Blaauwen, M.A.de Pedro, M.Nguyen-Distèche, and J.A.Ayala (2008).
Morphogenesis of rod-shaped sacculi.
  FEMS Microbiol Rev, 32, 321-344.  
17307852 B.D.Corbin, Y.Wang, T.K.Beuria, and W.Margolin (2007).
Interaction between cell division proteins FtsE and FtsZ.
  J Bacteriol, 189, 3026-3035.  
16352817 M.Vicente, A.I.Rico, R.Martínez-Arteaga, and J.Mingorance (2006).
Septum enlightenment: assembly of bacterial division proteins.
  J Bacteriol, 188, 19-27.  
16796675 S.Ishikawa, Y.Kawai, K.Hiramatsu, M.Kuwano, and N.Ogasawara (2006).
A new FtsZ-interacting protein, YlmF, complements the activity of FtsA during progression of cell division in Bacillus subtilis.
  Mol Microbiol, 60, 1364-1380.  
16194242 B.Geissler, and W.Margolin (2005).
Evidence for functional overlap among multiple bacterial cell division proteins: compensating for the loss of FtsK.
  Mol Microbiol, 58, 596-612.  
15630023 N.W.Goehring, F.Gueiros-Filho, and J.Beckwith (2005).
Premature targeting of a cell division protein to midcell allows dissection of divisome assembly in Escherichia coli.
  Genes Dev, 19, 127-137.  
  16511026 S.G.Addinall, K.A.Johnson, T.Dafforn, C.Smith, A.Rodger, R.P.Gomez, K.Sloan, A.Blewett, D.J.Scott, and D.I.Roper (2005).
Expression, purification and crystallization of the cell-division protein YgfE from Escherichia coli.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 305-307.  
16159787 S.O.Jensen, L.S.Thompson, and E.J.Harry (2005).
Cell division in Bacillus subtilis: FtsZ and FtsA association is Z-ring independent, and FtsA is required for efficient midcell Z-Ring assembly.
  J Bacteriol, 187, 6536-6544.  
15897178 T.A.Leonard, J.Møller-Jensen, and J.Löwe (2005).
Towards understanding the molecular basis of bacterial DNA segregation.
  Philos Trans R Soc Lond B Biol Sci, 360, 523-535.  
16227976 W.Margolin (2005).
FtsZ and the division of prokaryotic cells and organelles.
  Nat Rev Mol Cell Biol, 6, 862-871.  
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.