PDBsum entry 1o50

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protein links
Transferase PDB id
Protein chain
141 a.a. *
Waters ×214
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of a cbs domain-containing protein (tm0935 thermotoga maritima at 1.87 a resolution
Structure: Cbs domain-containing predicted protein tm0935. Chain: a. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: tm0935. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PDB file)
1.87Å     R-factor:   0.194     R-free:   0.255
Authors: Joint Center For Structural Genomics (Jcsg)
Key ref:
M.D.Miller et al. (2004). Crystal structure of a tandem cystathionine-beta-synthase (CBS) domain protein (TM0935) from Thermotoga maritima at 1.87 A resolution. Proteins, 57, 213-217. PubMed id: 15326606 DOI: 10.1002/prot.20024
31-Jul-03     Release date:   12-Aug-03    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q9X033  (Q9X033_THEMA) -  Histidine kinase
145 a.a.
141 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     phosphorylation   1 term 
  Biochemical function     catalytic activity     3 terms  


DOI no: 10.1002/prot.20024 Proteins 57:213-217 (2004)
PubMed id: 15326606  
Crystal structure of a tandem cystathionine-beta-synthase (CBS) domain protein (TM0935) from Thermotoga maritima at 1.87 A resolution.
M.D.Miller, R.Schwarzenbacher, F.von Delft, P.Abdubek, E.Ambing, T.Biorac, L.S.Brinen, J.M.Canaves, J.Cambell, H.J.Chiu, X.Dai, A.M.Deacon, M.DiDonato, M.A.Elsliger, S.Eshagi, R.Floyd, A.Godzik, C.Grittini, S.K.Grzechnik, E.Hampton, L.Jaroszewski, C.Karlak, H.E.Klock, E.Koesema, J.S.Kovarik, A.Kreusch, P.Kuhn, S.A.Lesley, I.Levin, D.McMullan, T.M.McPhillips, A.Morse, K.Moy, J.Ouyang, R.Page, K.Quijano, A.Robb, G.Spraggon, R.C.Stevens, H.van den Bedem, J.Velasquez, J.Vincent, X.Wang, B.West, G.Wolf, Q.Xu, K.O.Hodgson, J.Wooley, I.A.Wilson.
No abstract given.

  Selected figure(s)  
Figure 1.
Figure 1. Crystal structure of TM0935. (A) Stereo ribbon diagram of Thermotoga maritima TM0935 color coded from N-terminus (blue) to C-terminus (red) showing the domain organization. The helices H1-H6, -strands ( 1- 5) and the disordered residues 71 and 76 (dashed line) are indicated. Figure 1A produced with PYMOL (DeLano Scientific LLC). (B) Diagram showing the secondary structure elements in TM0935 superimposed on its primary sequence. -Hairpins are depicted in red and the -strands making up the two -sheets (A and B) are labeled. The disordered region is depicted in a dashed line with the corresponding sequence in brackets. Figure 1B adapted from PDBsum (
Figure 2.
Figure 2. (A) Ribbon diagram of the TM0935 dimer. (B) Ribbon diagram of a superposition of TM0935 (rainbow) and the CBS domain (residues 87-214) of IMPDH from Streptococcus pyogenes (gray). Helices and -strands are indicated for TM0935. Figures produced with PYMOL (DeLano Scientific LLC).
  The above figures are reprinted by permission from John Wiley & Sons, Inc.: Proteins (2004, 57, 213-217) copyright 2004.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19329426 N.A.Mahmood, E.Biemans-Oldehinkel, and B.Poolman (2009).
Engineering of Ion Sensing by the Cystathionine {beta}-Synthase Module of the ABC Transporter OpuA.
  J Biol Chem, 284, 14368-14376.  
  18765915 B.C.Jeong, K.S.Yoo, K.W.Jung, J.S.Shin, and H.K.Song (2008).
Purification, crystallization and preliminary X-ray diffraction analysis of a cystathionine beta-synthase domain-containing protein, CDCP2, from Arabidopsis thaliana.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 825-827.  
18648499 G.Q.Martinez, and M.Maduke (2008).
A cytoplasmic domain mutation in ClC-Kb affects long-distance communication across the membrane.
  PLoS ONE, 3, e2746.  
18312263 M.Pimkin, and G.D.Markham (2008).
The CBS subdomain of inosine 5'-monophosphate dehydrogenase regulates purine nucleotide turnover.
  Mol Microbiol, 68, 342-359.  
18021800 M.Proudfoot, S.A.Sanders, A.Singer, R.Zhang, G.Brown, A.Binkowski, L.Xu, J.A.Lukin, A.G.Murzin, A.Joachimiak, C.H.Arrowsmith, A.M.Edwards, A.V.Savchenko, and A.F.Yakunin (2008).
Biochemical and structural characterization of a novel family of cystathionine beta-synthase domain proteins fused to a Zn ribbon-like domain.
  J Mol Biol, 375, 301-315.
PDB codes: 1pvm 2qh1
18076763 N.Kannan, J.Wu, G.S.Anand, S.Yooseph, A.F.Neuwald, C.J.Venter, and S.S.Taylor (2007).
Evolution of allostery in the cyclic nucleotide binding module.
  Genome Biol, 8, R264.  
17452784 P.Day, A.Sharff, L.Parra, A.Cleasby, M.Williams, S.Hörer, H.Nar, N.Redemann, I.Tickle, and J.Yon (2007).
Structure of a CBS-domain pair from the regulatory gamma1 subunit of human AMPK in complex with AMP and ZMP.
  Acta Crystallogr D Biol Crystallogr, 63, 587-596.
PDB codes: 2uv4 2uv5 2uv6 2uv7
17289942 R.Townley, and L.Shapiro (2007).
Crystal structures of the adenylate sensor from fission yeast AMP-activated protein kinase.
  Science, 315, 1726-1729.
PDB codes: 2oox 2ooy
17562318 S.Markovic, and R.Dutzler (2007).
The structure of the cytoplasmic domain of the chloride channel ClC-Ka reveals a conserved interaction interface.
  Structure, 15, 715-725.
PDB code: 2pfi
16815971 E.Biemans-Oldehinkel, N.A.Mahmood, and B.Poolman (2006).
A sensor for intracellular ionic strength.
  Proc Natl Acad Sci U S A, 103, 10624-10629.  
16844687 N.A.Mahmood, E.Biemans-Oldehinkel, J.S.Patzlaff, G.K.Schuurman-Wolters, and B.Poolman (2006).
Ion specificity and ionic strength dependence of the osmoregulatory ABC transporter OpuA.
  J Biol Chem, 281, 29830-29839.  
17064285 S.B.Conners, E.F.Mongodin, M.R.Johnson, C.I.Montero, K.E.Nelson, and R.M.Kelly (2006).
Microbial biochemistry, physiology, and biotechnology of hyperthermophilic Thermotoga species.
  FEMS Microbiol Rev, 30, 872-905.  
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.