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PDBsum entry 1k69

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protein ligands Protein-protein interface(s) links
Ligase PDB id
1k69

 

 

 

 

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Contents
Protein chains
79 a.a.
447 a.a.
Ligands
BTN
ATP
Theoretical model
PDB id:
1k69
Name: Ligase
Title: Model interaction between bccp and atp-bound carboxylase subunit of acetyl coa carboxylase
Structure: Biotin carboxyl carrier protein of acetyl-coa carboxylase. Chain: b. Synonym: bccp. Other_details: from PDB entry 1bdo. Biotin carboxylase. Chain: a. Synonym: acc, a subunit of acetyl-coa carboxylase. Other_details: from PDB entry 1dv2
Source: Escherichia coli. Bacteria. Bacteria
Authors: L.H.Weaver,K.Kwon,D.Beckett,B.W.Matthews
Key ref: L.H.Weaver et al. (2001). Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor. Protein Sci, 10, 2618-2622. PubMed id: 11714930
Date:
15-Oct-01     Release date:   05-Dec-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
P02905  (BCCP_ECOLI) - 
Protein chain
Pfam   ArchSchema ?
P24182  (ACCC_ECOLI) -  Biotin carboxylase
Seq:
Struc:
449 a.a.
447 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: Chain A: E.C.6.3.4.14  - biotin carboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: N6-biotinyl-L-lysyl-[protein] + hydrogencarbonate + ATP = N6- carboxybiotinyl-L-lysyl-[protein] + ADP + phosphate + H+
N(6)-biotinyl-L-lysyl-[protein]
+ hydrogencarbonate
+ ATP
= N(6)- carboxybiotinyl-L-lysyl-[protein]
Bound ligand (Het Group name = ATP)
matches with 8710.00% similarity corresponds exactly
+ ADP
+ phosphate
+ H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Protein Sci 10:2618-2622 (2001)
PubMed id: 11714930  
 
 
Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor.
L.H.Weaver, K.Kwon, D.Beckett, B.W.Matthews.
 
  ABSTRACT  
 
A model is suggested for the complex between the biotin repressor of Escherichia coli, BirA, and BCCP, the biotin carboxyl carrier protein to which BirA transfers biotin. The model is consistent with prior physical and biochemical studies. Measurement of transfer rates for variants of BirA with single-site mutations in the proposed BirA:BCCP interface region also provides support. The unique feature of the proposed interaction between BirA and BCCP is that it uses the same beta-sheet region on the surface of BirA that the protein uses for homodimerization into a form competent to bind DNA. The resulting mutually exclusive protein:protein interfaces explain the novel feature of the BirA regulatory system, namely, that transcription of the genes involved in biotin synthesis is not determined by the level of biotin, per se, but by the level of unmodified BCCP. The model also provides a role for the C-terminal domain of BirA that is structurally similar to an SH3 domain.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
21056114 P.Handke, S.A.Lynch, and R.T.Gill (2011).
Application and engineering of fatty acid biosynthesis in Escherichia coli for advanced fuels and chemicals.
  Metab Eng, 13, 28-37.  
20142036 J.Solbiati, and J.E.Cronan (2010).
The switch regulating transcription of the Escherichia coli biotin operon does not require extensive protein-protein interactions.
  Chem Biol, 17, 11-17.  
  19056812 D.Beckett (2009).
Biotin sensing at the molecular level.
  J Nutr, 139, 167-170.  
19361526 H.Zhao, S.Naganathan, and D.Beckett (2009).
Thermodynamic and structural investigation of bispecificity in protein-protein interactions.
  J Mol Biol, 389, 336-348.  
19157941 Y.I.Hassan, H.Moriyama, L.J.Olsen, X.Bi, and J.Zempleni (2009).
N- and C-terminal domains in human holocarboxylase synthetase participate in substrate recognition.
  Mol Genet Metab, 96, 183-188.  
18508076 H.Zhao, and D.Beckett (2008).
Kinetic partitioning between alternative protein-protein interactions controls a transcriptional switch.
  J Mol Biol, 380, 223-236.  
18396082 J.R.Bernstein, T.Bulter, and J.C.Liao (2008).
Transfer of the high-GC cyclohexane carboxylate degradation pathway from Rhodopseudomonas palustris to Escherichia coli for production of biotin.
  Metab Eng, 10, 131-140.  
17056747 A.M.Abdel-Hamid, and J.E.Cronan (2007).
Coordinate expression of the acetyl coenzyme A carboxylase genes, accB and accC, is necessary for normal regulation of biotin synthesis in Escherichia coli.
  J Bacteriol, 189, 369-376.  
  17401210 B.Bagautdinov, Y.Matsuura, S.Bagautdinova, and N.Kunishima (2007).
Crystallization and preliminary X-ray crystallographic studies of the biotin carboxyl carrier protein and biotin protein ligase complex from Pyrococcus horikoshii OT3.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 63, 334-337.  
17468269 E.Leonard, K.H.Lim, P.N.Saw, and M.A.Koffas (2007).
Engineering central metabolic pathways for high-level flavonoid production in Escherichia coli.
  Appl Environ Microbiol, 73, 3877-3886.  
16823034 E.D.Streaker, and D.Beckett (2006).
Nonenzymatic biotinylation of a biotin carboxyl carrier protein: unusual reactivity of the physiological target lysine.
  Protein Sci, 15, 1928-1935.  
16204850 D.Beckett (2005).
Multilevel regulation of protein-protein interactions in biological circuitry.
  Phys Biol, 2, S67-S73.  
15992680 D.Beckett (2005).
The Escherichia coli biotin regulatory system: a transcriptional switch.
  J Nutr Biochem, 16, 411-415.  
15459338 E.Choi-Rhee, H.Schulman, and J.E.Cronan (2004).
Promiscuous protein biotinylation by Escherichia coli biotin protein ligase.
  Protein Sci, 13, 3043-3050.  
12631286 D.J.Clarke, J.Coulson, R.Baillie, and D.J.Campopiano (2003).
Biotinylation in the hyperthermophile Aquifex aeolicus.
  Eur J Biochem, 270, 1277-1287.  
11847279 K.Kwon, E.D.Streaker, and D.Beckett (2002).
Binding specificity and the ligand dissociation process in the E. coli biotin holoenzyme synthetase.
  Protein Sci, 11, 558-570.  
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.

 

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