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PDBsum entry 1qh4

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protein ligands metals Protein-protein interface(s) links
Transferase PDB id
1qh4
Jmol
Contents
Protein chains
380 a.a. *
Ligands
ACT ×6
Metals
_CA
Waters ×1467
* Residue conservation analysis
PDB id:
1qh4
Name: Transferase
Title: Crystal structure of chicken brain-type creatine kinase at 1.41 angstrom resolution
Structure: Creatine kinase. Chain: a, b, c, d. Fragment: b chain. Synonym: bb-ck, brain-type creatine kinase. Engineered: yes
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Organ: brain. Cellular_location: cytoplasm. Gene: embl-nr. X03509. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
1.41Å     R-factor:   0.137     R-free:   0.188
Authors: M.Eder,U.Schlattner,A.Becker,T.Wallimann,W.Kabsch,K.Fritz- Wolf
Key ref: M.Eder et al. (1999). Crystal structure of brain-type creatine kinase at 1.41 A resolution. Protein Sci, 8, 2258-2269. PubMed id: 10595529 DOI: 10.1110/ps.8.11.2258
Date:
11-May-99     Release date:   19-Nov-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P05122  (KCRB_CHICK) -  Creatine kinase B-type
Seq:
Struc:
381 a.a.
380 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.7.3.2  - Creatine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway:
Creatine Biosynthesis
      Reaction: ATP + creatine = ADP + phosphocreatine
ATP
+
creatine
Bound ligand (Het Group name = ACT)
matches with 44.00% similarity
= ADP
+ phosphocreatine
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     cytoplasm   1 term 
  Biological process     phosphorylation   1 term 
  Biochemical function     catalytic activity     7 terms  

 

 
    reference    
 
 
DOI no: 10.1110/ps.8.11.2258 Protein Sci 8:2258-2269 (1999)
PubMed id: 10595529  
 
 
Crystal structure of brain-type creatine kinase at 1.41 A resolution.
M.Eder, U.Schlattner, A.Becker, T.Wallimann, W.Kabsch, K.Fritz-Wolf.
 
  ABSTRACT  
 
Excitable cells and tissues like muscle or brain show a highly fluctuating consumption of ATP, which is efficiently regenerated from a large pool of phosphocreatine by the enzyme creatine kinase (CK). The enzyme exists in tissue--as well as compartment-specific isoforms. Numerous pathologies are related to the CK system: CK is found to be overexpressed in a wide range of solid tumors, whereas functional impairment of CK leads to a deterioration in energy metabolism, which is phenotypic for many neurodegenerative and age-related diseases. The crystal structure of chicken cytosolic brain-type creatine kinase (BB-CK) has been solved to 1.41 A resolution by molecular replacement. It represents the most accurately determined structure in the family of guanidino kinases. Except for the N-terminal region (2-12), the structures of both monomers in the biological dimer are very similar and closely resemble those of the other known structures in the family. Specific Ca2+-mediated interactions, found between two dimers in the asymmetric unit, result in structurally independent heterodimers differing in their N-terminal conformation and secondary structure. The high-resolution structure of BB-CK presented in this work will assist in designing new experiments to reveal the molecular basis of the multiple isoform-specific properties of CK, especially regarding different subcellular locations and functional interactions with other proteins. The rather similar fold shared by all known guanidino kinase structures suggests a model for the transition state complex of BB-CK analogous to the one of arginine kinase (AK). Accordingly, we have modeled a putative conformation of CK in the transition state that requires a rigid body movement of the entire N-terminal domain by rms 4 A from the structure without substrates.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  18765922 A.M.Awama, P.Paracuellos, S.Laurent, C.Dissous, O.Marcillat, and P.Gouet (2008).
Crystallization and X-ray analysis of the Schistosoma mansoni guanidino kinase.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 854-857.  
18190534 G.G.Hoffman, O.Davulcu, S.Sona, and W.R.Ellington (2008).
Contributions to catalysis and potential interactions of the three catalytic domains in a contiguous trimeric creatine kinase.
  FEBS J, 275, 646-654.  
17327675 J.F.Ohren, M.L.Kundracik, C.L.Borders, P.Edmiston, and R.E.Viola (2007).
Structural asymmetry and intersubunit communication in muscle creatine kinase.
  Acta Crystallogr D Biol Crystallogr, 63, 381-389.  
17036164 T.S.Bürklen, A.Hirschy, and T.Wallimann (2007).
Brain-type creatine kinase BB-CK interacts with the Golgi Matrix Protein GM130 in early prophase.
  Mol Cell Biochem, 297, 53-64.  
16103910 B.E.Shakhnovich (2005).
Improving the precision of the structure-function relationship by considering phylogenetic context.
  PLoS Comput Biol, 1, e9.  
16006628 H.W.He, J.Zhang, H.M.Zhou, and Y.B.Yan (2005).
Conformational change in the C-terminal domain is responsible for the initiation of creatine kinase thermal aggregation.
  Biophys J, 89, 2650-2658.  
15211520 C.Lehmann, V.Doseeva, S.Pullalarevu, W.Krajewski, A.Howard, and O.Herzberg (2004).
YbdK is a carboxylate-amine ligase with a gamma-glutamyl:Cysteine ligase activity: crystal structure and enzymatic assays.
  Proteins, 56, 376-383.
PDB code: 1r8g
15215531 J.C.Pan, Z.Yu, X.Y.Su, Y.Q.Sun, X.M.Rao, and H.M.Zhou (2004).
Unassisted refolding of urea-denatured arginine kinase from shrimp Feneropenaeus chinensis: evidence for two equilibrium intermediates in the refolding pathway.
  Protein Sci, 13, 1892-1901.  
12592023 C.L.Borders, K.M.MacGregor, P.L.Edmiston, E.R.Gbeddy, M.J.Thomenius, G.B.Mulligan, and M.J.Snider (2003).
Asparagine 285 plays a key role in transition state stabilization in rabbit muscle creatine kinase.
  Protein Sci, 12, 532-537.  
12493833 M.S.Yousef, S.A.Clark, P.K.Pruett, T.Somasundaram, W.R.Ellington, and M.S.Chapman (2003).
Induced fit in guanidino kinases--comparison of substrate-free and transition state analog structures of arginine kinase.
  Protein Sci, 12, 103-111.
PDB code: 1m80
12454458 M.S.Yousef, F.Fabiola, J.L.Gattis, T.Somasundaram, and M.S.Chapman (2002).
Refinement of the arginine kinase transition-state analogue complex at 1.2 A resolution: mechanistic insights.
  Acta Crystallogr D Biol Crystallogr, 58, 2009-2017.
PDB code: 1m15
11173463 D.Tisi, B.Bax, and A.Loew (2001).
The three-dimensional structure of cytosolic bovine retinal creatine kinase.
  Acta Crystallogr D Biol Crystallogr, 57, 187-193.
PDB code: 1g0w
11258919 J.S.Cantwell, W.R.Novak, P.F.Wang, M.J.McLeish, G.L.Kenyon, and P.C.Babbitt (2001).
Mutagenesis of two acidic active site residues in human muscle creatine kinase: implications for the catalytic mechanism.
  Biochemistry, 40, 3056-3061.  
10737943 M.Eder, K.Fritz-Wolf, W.Kabsch, T.Wallimann, and U.Schlattner (2000).
Crystal structure of human ubiquitous mitochondrial creatine kinase.
  Proteins, 39, 216-225.
PDB code: 1qk1
10851020 T.Hornemann, M.Stolz, and T.Wallimann (2000).
Isoenzyme-specific interaction of muscle-type creatine kinase with the sarcomeric M-line is mediated by NH(2)-terminal lysine charge-clamps.
  J Cell Biol, 149, 1225-1234.  
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 code is shown on the right.