PDBsum entry 1xnf

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Structural genomics, unknown function PDB id
Protein chains
259 a.a. *
TRS ×2
Waters ×436
* Residue conservation analysis
PDB id:
Name: Structural genomics, unknown function
Title: Crystal structure of e.Coli tpr-protein nlpi
Structure: Lipoprotein nlpi. Chain: a, b. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562. Gene: nlpi. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
Biol. unit: Dimer (from PQS)
1.98Å     R-factor:   0.171     R-free:   0.206
Authors: C.G.Wilson,T.Kajander,L.Regan
Key ref:
C.G.Wilson et al. (2005). The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold. FEBS J, 272, 166-179. PubMed id: 15634341 DOI: 10.1111/j.1432-1033.2004.04397.x
04-Oct-04     Release date:   16-Nov-04    
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Protein chains
Pfam   ArchSchema ?
P0AFB1  (NLPI_ECOLI) -  Lipoprotein NlpI
294 a.a.
259 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   2 terms 
  Biological process     cell cycle   2 terms 


DOI no: 10.1111/j.1432-1033.2004.04397.x FEBS J 272:166-179 (2005)
PubMed id: 15634341  
The crystal structure of NlpI. A prokaryotic tetratricopeptide repeat protein with a globular fold.
C.G.Wilson, T.Kajander, L.Regan.
There are several different families of repeat proteins. In each, a distinct structural motif is repeated in tandem to generate an elongated structure. The nonglobular, extended structures that result are particularly well suited to present a large surface area and to function as interaction domains. Many repeat proteins have been demonstrated experimentally to fold and function as independent domains. In tetratricopeptide (TPR) repeats, the repeat unit is a helix-turn-helix motif. The majority of TPR motifs occur as three to over 12 tandem repeats in different proteins. The majority of TPR structures in the Protein Data Bank are of isolated domains. Here we present the high-resolution structure of NlpI, the first structure of a complete TPR-containing protein. We show that in this instance the TPR motifs do not fold and function as an independent domain, but are fully integrated into the three-dimensional structure of a globular protein. The NlpI structure is also the first TPR structure from a prokaryote. It is of particular interest because it is a membrane-associated protein, and mutations in it alter septation and virulence.
  Selected figure(s)  
Figure 3.
Fig. 3. Sample 2Fo-Fc density map for NlpI (sigma = 1.0). Residues shown are Gln158-Asn162 (QDDPN) for chain A, which corresponds to the turn region between helices 7 and 8. Image was produced with BOBSCRIPT[57] and RASTER3D[58].
Figure 7.
Fig. 7. Structural homologues of NlpI. Structure alignment of NlpI (blue) with (A) p67^phox and (B) domain III of MalT (yellow). Superimposition of coordinates was performed with LSQ_EXPLICIT and LSQ_IMPROVE[45].
  The above figures are reprinted by permission from the Federation of European Biochemical Societies: FEBS J (2005, 272, 166-179) copyright 2005.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21308846 A.Eichinger, I.Haneburger, C.Koller, K.Jung, and A.Skerra (2011).
Crystal structure of the sensory domain of Escherichia coli CadC, a member of the ToxR-like protein family.
  Protein Sci, 20, 656-669.
PDB codes: 3ly7 3ly8 3ly9 3lya
21204920 R.Hoge, M.Laschinski, K.E.Jaeger, S.Wilhelm, and F.Rosenau (2011).
The subcellular localization of a C-terminal processing protease in Pseudomonas aeruginosa.
  FEMS Microbiol Lett, 316, 23-30.  
20421385 C.H.Teng, Y.T.Tseng, R.Maruvada, D.Pearce, Y.Xie, M.Paul-Satyaseela, and K.S.Kim (2010).
NlpI contributes to Escherichia coli K1 strain RS218 interaction with human brain microvascular endothelial cells.
  Infect Immun, 78, 3090-3096.  
19091741 D.Han, K.Kim, Y.Kim, Y.Kang, J.Y.Lee, and Y.Kim (2009).
Crystal structure of the N-terminal domain of anaphase-promoting complex subunit 7.
  J Biol Chem, 284, 15137-15146.
PDB code: 3ffl
17803240 D.Han, K.Kim, J.Oh, J.Park, and Y.Kim (2008).
TPR domain of NrfG mediates complex formation between heme lyase and formate-dependent nitrite reductase in Escherichia coli O157:H7.
  Proteins, 70, 900-914.
PDB code: 2e2e
17634984 M.Palaiomylitou, A.Tartas, D.Vlachakis, D.Tzamarias, and M.Vlassi (2008).
Investigating the structural stability of the Tup1-interaction domain of Ssn6: evidence for a conformational change on the complex.
  Proteins, 70, 72-82.  
17371850 G.Parthasarathy, Y.Yao, and K.S.Kim (2007).
Flagella promote Escherichia coli K1 association with and invasion of human brain microvascular endothelial cells.
  Infect Immun, 75, 2937-2945.  
16855227 A.J.McBroom, A.P.Johnson, S.Vemulapalli, and M.J.Kuehn (2006).
Outer membrane vesicle production by Escherichia coli is independent of membrane instability.
  J Bacteriol, 188, 5385-5392.  
16359316 P.J.Edqvist, J.E.Bröms, H.J.Betts, A.Forsberg, M.J.Pallen, and M.S.Francis (2006).
Tetratricopeptide repeats in the type III secretion chaperone, LcrH: their role in substrate binding and secretion.
  Mol Microbiol, 59, 31-44.  
16040755 V.M.Bolanos-Garcia, S.Beaufils, A.Renault, J.G.Grossmann, S.Brewerton, M.Lee, A.Venkitaraman, and T.L.Blundell (2005).
The conserved N-terminal region of the mitotic checkpoint protein BUBR1: a putative TPR motif of high surface activity.
  Biophys J, 89, 2640-2649.  
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.