PDBsum entry 1zx8

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protein ligands metals Protein-protein interface(s) links
Unknown function PDB id
Protein chains
127 a.a. *
1PE ×3
Waters ×243
* Residue conservation analysis
PDB id:
Name: Unknown function
Title: Crystal structure of an atypical cyclophilin (peptidylprolyl isomerase) (tm1367) from thermotoga maritima at 1.90 a reso
Structure: Hypothetical protein tm1367. Chain: a, b, c. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: tm1367. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.90Å     R-factor:   0.166     R-free:   0.210
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref:
K.K.Jin et al. (2006). Crystal structure of TM1367 from Thermotoga maritima at 1.90 A resolution reveals an atypical member of the cyclophilin (peptidylprolyl isomerase) fold. Proteins, 63, 1112-1118. PubMed id: 16544291 DOI: 10.1002/prot.20894
07-Jun-05     Release date:   26-Jul-05    
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Protein chains
Pfam   ArchSchema ?
Q9X187  (Q9X187_THEMA) -  DUF369 domain-containing protein
124 a.a.
127 a.a.
Key:    PfamA domain  Secondary structure


DOI no: 10.1002/prot.20894 Proteins 63:1112-1118 (2006)
PubMed id: 16544291  
Crystal structure of TM1367 from Thermotoga maritima at 1.90 A resolution reveals an atypical member of the cyclophilin (peptidylprolyl isomerase) fold.
K.K.Jin, S.S.Krishna, R.Schwarzenbacher, D.McMullan, P.Abdubek, S.Agarwalla, E.Ambing, H.Axelrod, J.M.Canaves, H.J.Chiu, A.M.Deacon, M.DiDonato, M.A.Elsliger, J.Feuerhelm, A.Godzik, C.Grittini, S.K.Grzechnik, J.Hale, E.Hampton, J.Haugen, M.Hornsby, L.Jaroszewski, H.E.Klock, M.W.Knuth, E.Koesema, A.Kreusch, P.Kuhn, S.A.Lesley, M.D.Miller, K.Moy, E.Nigoghossian, L.Okach, S.Oommachen, J.Paulsen, K.Quijano, R.Reyes, C.Rife, R.C.Stevens, G.Spraggon, H.van den Bedem, J.Velasquez, A.White, G.Wolf, G.W.Han, Q.Xu, K.O.Hodgson, J.Wooley, I.A.Wilson.
No abstract given.

  Selected figure(s)  
Figure 2.
Figure 2. A: Structural superposition of TM1367 (blue) and the human cyclophilin A (PDB: 2cpl, gray). Residues corresponding to the calcineurin binding site of human cyclophilin A are shown in ball-and-stick representation. B: Residues corresponding to PPlase active site of cyclophilin A are shown in ball-and-stick representation. TM1367 residues are shown in brackets.
Figure 3.
Figure 3. A: Structure of TM1367 with a PEG-200 molecule in the putative active site. Contact residues of chain B in a shell 4 Å from the PEG molecule are shown in ball-and-stick. B: Structural superposition of TM1367 (blue) and the C-terminal domain of a protein of unknown function from B. cereus (PDB: 1×7f, green), which is a seven- rather than eight-stranded, closed -barrel.
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2006, 63, 1112-1118) copyright 2006.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
  20944235 B.Mohanty, P.Serrano, B.Pedrini, K.Jaudzems, M.Geralt, R.Horst, T.Herrmann, M.A.Elsliger, I.A.Wilson, and K.Wüthrich (2010).
Comparison of NMR and crystal structures for the proteins TM1112 and TM1367.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 66, 1381-1392.
PDB codes: 2k9z 2ka0
19465773 T.C.Terwilliger, P.D.Adams, R.J.Read, A.J.McCoy, N.W.Moriarty, R.W.Grosse-Kunstleve, P.V.Afonine, P.H.Zwart, and L.W.Hung (2009).
Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard.
  Acta Crystallogr D Biol Crystallogr, 65, 582-601.  
18073103 W.A.Hendrickson (2007).
Impact of structures from the protein structure initiative.
  Structure, 15, 1528-1529.  
17206469 X.Ai, A.Semesi, A.Yee, C.H.Arrowsmith, S.S.Li, and W.Y.Choy (2007).
Backbone and side chain 1H, 13C, and 15N resonance assignments of AF2241 from Archaeoglobus fulgidus.
  J Biomol NMR, 38, 183.  
17610131 X.Ai, L.Li, A.Semesi, A.Yee, C.H.Arrowsmith, S.S.Li, and W.Y.Choy (2007).
Hypothetical protein AF2241 from Archaeoglobus fulgidus adopts a cyclophilin-like fold.
  J Biomol NMR, 38, 353-358.
PDB code: 2nnz
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