PDBsum entry 1bnc

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Fatty acid biosynthesis PDB id
Protein chains
433 a.a. *
PO4 ×2
Waters ×116
* Residue conservation analysis
PDB id:
Name: Fatty acid biosynthesis
Title: Three-dimensional structure of the biotin carboxylase subunit of acetyl-coa carboxylase
Structure: Biotin carboxylase. Chain: a, b. Ec:
Source: Escherichia coli. Organism_taxid: 562
Biol. unit: Dimer (from PQS)
2.40Å     R-factor:   0.183    
Authors: G.Waldrop,I.Rayment,H.M.Holden
Key ref:
G.L.Waldrop et al. (1994). Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase. Biochemistry, 33, 10249-10256. PubMed id: 7915138 DOI: 10.1021/bi00200a004
06-Jul-94     Release date:   30-Aug-95    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P24182  (ACCC_ECOLI) -  Biotin carboxylase
449 a.a.
433 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class 1: E.C.  - Biotin carboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + biotin-[carboxyl-carrier-protein] + CO2 = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein]
+ biotin-[carboxyl-carrier-protein]
+ CO(2)
Bound ligand (Het Group name = PO4)
corresponds exactly
+ carboxy-biotin-[carboxyl-carrier-protein]
   Enzyme class 2: E.C.  - Acetyl-CoA carboxylase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + acetyl-CoA + HCO3- = ADP + phosphate + malonyl-CoA
+ acetyl-CoA
+ HCO(3)(-)
Bound ligand (Het Group name = PO4)
corresponds exactly
+ malonyl-CoA
      Cofactor: Biotin
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
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     metabolic process   6 terms 
  Biochemical function     catalytic activity     8 terms  


DOI no: 10.1021/bi00200a004 Biochemistry 33:10249-10256 (1994)
PubMed id: 7915138  
Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase.
G.L.Waldrop, I.Rayment, H.M.Holden.
Acetyl-CoA carboxylase is found in all animals, plants, and bacteria and catalyzes the first committed step in fatty acid synthesis. It is a multicomponent enzyme containing a biotin carboxylase activity, a biotin carboxyl carrier protein, and a carboxyltransferase functionality. Here we report the X-ray structure of the biotin carboxylase component from Escherichia coli determined to 2.4-A resolution. The structure was solved by a combination of multiple isomorphous replacement and electron density modification procedures. The overall fold of the molecule may be described in terms of three structural domains. The N-terminal region, formed by Met 1-Ile 103, adopts a dinucleotide binding motif with five strands of parallel beta-sheet flanked on either side by alpha-helices. The "B-domain" extends from the main body of the subunit where it folds into two alpha-helical regions and three strands of beta-sheet. Following the excursion into the B-domain, the polypeptide chain folds back into the body of the protein where it forms an eight-stranded antiparallel beta-sheet. In addition to this major secondary structural element, the C-terminal domain also contains a smaller three-stranded antiparallel beta-sheet and seven alpha-helices. The active site of the enzyme has been identified tentatively by a difference Fourier map calculated between X-ray data from the native crystals and from crystals soaked in a Ag+/biotin complex. Those amino acid residues believed to form part of the active site pocket include His 209-Glu 211, His 236-Glu 241, Glu 276, Ile 287-Glu 296, and Arg 338.2+ represents the first X-ray model of a biotin-dependent carboxylase.

Literature references that cite this PDB file's key reference

  PubMed id Reference
21204864 G.Gago, L.Diacovich, A.Arabolaza, S.C.Tsai, and H.Gramajo (2011).
Fatty acid biosynthesis in actinomycetes.
  FEMS Microbiol Rev, 35, 475-497.  
21097780 U.Pieper, B.M.Webb, D.T.Barkan, D.Schneidman-Duhovny, A.Schlessinger, H.Braberg, Z.Yang, E.C.Meng, E.F.Pettersen, C.C.Huang, R.S.Datta, P.Sampathkumar, M.S.Madhusudhan, K.Sjölander, T.E.Ferrin, S.K.Burley, and A.Sali (2011).
ModBase, a database of annotated comparative protein structure models, and associated resources.
  Nucleic Acids Res, 39, D465-D474.  
20952656 C.L.Colbert, C.W.Kim, Y.A.Moon, L.Henry, M.Palnitkar, W.B.McKean, K.Fitzgerald, J.Deisenhofer, J.D.Horton, and H.J.Kwon (2010).
Crystal structure of Spot 14, a modulator of fatty acid synthesis.
  Proc Natl Acad Sci U S A, 107, 18820-18825.
PDB code: 3ont
20725044 C.S.Huang, K.Sadre-Bazzaz, Y.Shen, B.Deng, Z.H.Zhou, and L.Tong (2010).
Crystal structure of the alpha(6)beta(6) holoenzyme of propionyl-coenzyme A carboxylase.
  Nature, 466, 1001-1005.
PDB code: 3n6r
20142038 S.A.Borisova, B.T.Circello, J.K.Zhang, W.A.van der Donk, and W.W.Metcalf (2010).
Biosynthesis of rhizocticins, antifungal phosphonate oligopeptides produced by Bacillus subtilis ATCC6633.
  Chem Biol, 17, 28-37.  
20230056 S.Duangpan, S.Jitrapakdee, A.Adina-Zada, L.Byrne, T.N.Zeczycki, M.St Maurice, W.W.Cleland, J.C.Wallace, and P.V.Attwood (2010).
Probing the catalytic roles of Arg548 and Gln552 in the carboxyl transferase domain of the Rhizobium etli pyruvate carboxylase by site-directed mutagenesis.
  Biochemistry, 49, 3296-3304.  
19213731 C.Y.Chou, L.P.Yu, and L.Tong (2009).
Crystal structure of biotin carboxylase in complex with substrates and implications for its catalytic mechanism.
  J Biol Chem, 284, 11690-11697.
PDB codes: 3g8c 3g8d
19384989 H.Li, W.Fast, and S.J.Benkovic (2009).
Structural and functional modularity of proteins in the de novo purine biosynthetic pathway.
  Protein Sci, 18, 881-892.  
18725455 I.Mochalkin, J.R.Miller, A.Evdokimov, S.Lightle, C.Yan, C.K.Stover, and G.L.Waldrop (2008).
Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase.
  Protein Sci, 17, 1706-1718.
PDB codes: 2c00 2j9g 2vpq 2vqd 2vr1
18613815 S.Jitrapakdee, M.St Maurice, I.Rayment, W.W.Cleland, J.C.Wallace, and P.V.Attwood (2008).
Structure, mechanism and regulation of pyruvate carboxylase.
  Biochem J, 413, 369-387.  
18271571 S.O.Nilsson Lill, J.Gao, and G.L.Waldrop (2008).
Molecular dynamics simulations of biotin carboxylase.
  J Phys Chem B, 112, 3149-3156.  
17876819 Y.S.Cho, J.I.Lee, D.Shin, H.T.Kim, Y.H.Cheon, C.I.Seo, Y.E.Kim, Y.L.Hyun, Y.S.Lee, K.Sugiyama, S.Y.Park, S.Ro, J.M.Cho, T.G.Lee, and Y.S.Heo (2008).
Crystal structure of the biotin carboxylase domain of human acetyl-CoA carboxylase 2.
  Proteins, 70, 268-272.
PDB code: 2hjw
18712276 Y.Zhang, M.Morar, and S.E.Ealick (2008).
Structural biology of the purine biosynthetic pathway.
  Cell Mol Life Sci, 65, 3699-3724.  
18069798 Y.Zhang, R.H.White, and S.E.Ealick (2008).
Crystal structure and function of 5-formaminoimidazole-4-carboxamide ribonucleotide synthetase from Methanocaldococcus jannaschii.
  Biochemistry, 47, 205-217.
PDB codes: 2r7k 2r7l 2r7m 2r7n 2r84 2r85 2r86 2r87
17483212 R.Gande, L.G.Dover, K.Krumbach, G.S.Besra, H.Sahm, T.Oikawa, and L.Eggeling (2007).
The two carboxylases of Corynebacterium glutamicum essential for fatty acid and mycolic acid synthesis.
  J Bacteriol, 189, 5257-5264.  
17659996 S.Jitrapakdee, K.H.Surinya, A.Adina-Zada, S.W.Polyak, C.Stojkoski, R.Smyth, G.W.Booker, W.W.Cleland, P.V.Attwood, and J.C.Wallace (2007).
Conserved Glu40 and Glu433 of the biotin carboxylase domain of yeast pyruvate carboxylase I isoenzyme are essential for the association of tetramers.
  Int J Biochem Cell Biol, 39, 2120-2134.  
16983687 L.Tong, and H.J.Harwood (2006).
Acetyl-coenzyme A carboxylases: versatile targets for drug discovery.
  J Cell Biochem, 99, 1476-1488.  
16481318 M.E.Fraser, K.Hayakawa, M.S.Hume, D.G.Ryan, and E.R.Brownie (2006).
Interactions of GTP with the ATP-grasp domain of GTP-specific succinyl-CoA synthetase.
  J Biol Chem, 281, 11058-11065.
PDB codes: 2fp4 2fpg 2fpi 2fpp
16676358 M.Seki (2006).
Biological significance and development of practical synthesis of biotin.
  Med Res Rev, 26, 434-482.  
16793549 Y.Shen, C.Y.Chou, G.G.Chang, and L.Tong (2006).
Is dimerization required for the catalytic activity of bacterial biotin carboxylase?
  Mol Cell, 22, 807-818.
PDB codes: 2gps 2gpw
  16511069 J.Jeyakanthan, E.Inagaki, C.Kuroishi, and T.H.Tahirov (2005).
Structure of PIN-domain protein PH0500 from Pyrococcus horikoshii.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 463-468.
PDB codes: 1v96 1ye5
14612443 J.M.Rodríguez, P.Ruíz-Sala, M.Ugarte, and M.A.Peñalva (2004).
Fungal metabolic model for 3-methylcrotonyl-CoA carboxylase deficiency.
  J Biol Chem, 279, 4578-4587.  
  15043388 R.J.Heath, and C.O.Rock (2004).
Fatty acid biosynthesis as a target for novel antibacterials.
  Curr Opin Investig Drugs, 5, 146-153.  
15030490 S.Sueda, M.N.Islam, and H.Kondo (2004).
Protein engineering of pyruvate carboxylase: investigation on the function of acetyl-CoA and the quaternary structure.
  Eur J Biochem, 271, 1391-1400.  
15090492 T.Kanamori, N.Kanou, H.Atomi, and T.Imanaka (2004).
Enzymatic characterization of a prokaryotic urea carboxylase.
  J Bacteriol, 186, 2532-2539.  
14960587 V.Sloane, and G.L.Waldrop (2004).
Kinetic characterization of mutations found in propionic acidemia and methylcrotonylglycinuria: evidence for cooperativity in biotin carboxylase.
  J Biol Chem, 279, 15772-15778.  
15215578 Y.Sasaki, and Y.Nagano (2004).
Plant acetyl-CoA carboxylase: structure, biosynthesis, regulation, and gene manipulation for plant breeding.
  Biosci Biotechnol Biochem, 68, 1175-1184.  
15610732 Y.Shen, S.L.Volrath, S.C.Weatherly, T.D.Elich, and L.Tong (2004).
A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product.
  Mol Cell, 16, 881-891.
PDB codes: 1w93 1w96
12794081 E.Choi-Rhee, and J.E.Cronan (2003).
The biotin carboxylase-biotin carboxyl carrier protein complex of Escherichia coli acetyl-CoA carboxylase.
  J Biol Chem, 278, 30806-30812.  
12533469 S.Chuakrut, H.Arai, M.Ishii, and Y.Igarashi (2003).
Characterization of a bifunctional archaeal acyl coenzyme A carboxylase.
  J Bacteriol, 185, 938-947.  
12121720 J.E.Cronan, and G.L.Waldrop (2002).
Multi-subunit acetyl-CoA carboxylases.
  Prog Lipid Res, 41, 407-435.  
12005432 S.Ramón-Maiques, A.Marina, F.Gil-Ortiz, I.Fita, and V.Rubio (2002).
Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis.
  Structure, 10, 329-342.
PDB codes: 1gs5 1gsj
11714930 L.H.Weaver, K.Kwon, D.Beckett, and B.W.Matthews (2001).
Competing protein:protein interactions are proposed to control the biological switch of the E coli biotin repressor.
  Protein Sci, 10, 2618-2622.
PDB codes: 1k67 1k69
11170888 M.E.Gallardo, L.R.Desviat, J.M.Rodríguez, J.Esparza-Gordillo, C.Pérez-Cerdá, B.Pérez, P.Rodríguez-Pombo, O.Criado, R.Sanz, D.H.Morton, K.M.Gibson, T.P.Le, A.Ribes, Córdoba, M.Ugarte, and M.A.Peñalva (2001).
The molecular basis of 3-methylcrotonylglycinuria, a disorder of leucine catabolism.
  Am J Hum Genet, 68, 334-346.  
11181649 M.R.Baumgartner, S.Almashanu, T.Suormala, C.Obie, R.N.Cole, S.Packman, E.R.Baumgartner, and D.Valle (2001).
The molecular basis of human 3-methylcrotonyl-CoA carboxylase deficiency.
  J Clin Invest, 107, 495-504.  
11591436 R.J.Heath, S.W.White, and C.O.Rock (2001).
Lipid biosynthesis as a target for antibacterial agents.
  Prog Lipid Res, 40, 467-497.  
10713986 I.N.Shindyalov, and P.E.Bourne (2000).
An alternative view of protein fold space.
  Proteins, 38, 247-260.  
10821865 J.B.Thoden, C.Z.Blanchard, H.M.Holden, and G.L.Waldrop (2000).
Movement of the biotin carboxylase B-domain as a result of ATP binding.
  J Biol Chem, 275, 16183-16190.
PDB codes: 1dv1 1dv2
10913290 J.B.Thoden, S.Firestine, A.Nixon, S.J.Benkovic, and H.M.Holden (2000).
Molecular structure of Escherichia coli PurT-encoded glycinamide ribonucleotide transformylase.
  Biochemistry, 39, 8791-8802.
PDB codes: 1eyz 1ez1
10713991 K.A.Denessiouk, and M.S.Johnson (2000).
When fold is not important: a common structural framework for adenine and AMP binding in 12 unrelated protein families.
  Proteins, 38, 310-326.  
10747803 K.L.Levert, R.B.Lloyd, and G.L.Waldrop (2000).
Do cysteine 230 and lysine 238 of biotin carboxylase play a role in the activation of biotin?
  Biochemistry, 39, 4122-4128.  
10960111 S.Karlin, and J.Mrázek (2000).
Predicted highly expressed genes of diverse prokaryotic genomes.
  J Bacteriol, 182, 5238-5250.  
  10211841 A.Marina, P.M.Alzari, J.Bravo, M.Uriarte, B.Barcelona, I.Fita, and V.Rubio (1999).
Carbamate kinase: New structural machinery for making carbamoyl phosphate, the common precursor of pyrimidines and arginine.
  Protein Sci, 8, 934-940.
PDB codes: 1b7b 2we4 2we5
10508782 C.H.Weber, Y.S.Park, S.Sanker, C.Kent, and M.L.Ludwig (1999).
A prototypical cytidylyltransferase: CTP:glycerol-3-phosphate cytidylyltransferase from bacillus subtilis.
  Structure, 7, 1113-1124.
PDB code: 1coz
10508786 C.Li, T.J.Kappock, J.Stubbe, T.M.Weaver, and S.E.Ealick (1999).
X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5 A resolution.
  Structure, 7, 1155-1166.
PDB code: 1cli
10079084 C.Z.Blanchard, Y.M.Lee, P.A.Frantom, and G.L.Waldrop (1999).
Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin.
  Biochemistry, 38, 3393-3400.  
10074353 E.Meyer, T.J.Kappock, C.Osuji, and J.Stubbe (1999).
Evidence for the direct transfer of the carboxylate of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to generate 4-carboxy-5-aminoimidazole ribonucleotide catalyzed by Escherichia coli PurE, an N5-CAIR mutase.
  Biochemistry, 38, 3012-3018.  
10387030 F.M.Raushel, J.B.Thoden, and H.M.Holden (1999).
The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia.
  Biochemistry, 38, 7891-7899.  
10369661 G.Polekhina, P.G.Board, R.R.Gali, J.Rossjohn, and M.W.Parker (1999).
Molecular basis of glutathione synthetase deficiency and a rare gene permutation event.
  EMBO J, 18, 3204-3213.
PDB code: 2hgs
10574791 I.I.Mathews, T.J.Kappock, J.Stubbe, and S.E.Ealick (1999).
Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway.
  Structure, 7, 1395-1406.
PDB codes: 1d7a 1qcz
10089390 J.B.Thoden, F.M.Raushel, M.M.Benning, I.Rayment, and H.M.Holden (1999).
The structure of carbamoyl phosphate synthetase determined to 2.1 A resolution.
  Acta Crystallogr D Biol Crystallogr, 55, 8.
PDB code: 1jdb
10029528 J.B.Thoden, G.Wesenberg, F.M.Raushel, and H.M.Holden (1999).
Carbamoyl phosphate synthetase: closure of the B-domain as a result of nucleotide binding.
  Biochemistry, 38, 2347-2357.
PDB code: 1bxr
10103026 M.Kobayashi, and S.Shimizu (1999).
Cobalt proteins.
  Eur J Biochem, 261, 1-9.  
10347186 M.Uriarte, A.Marina, S.Ramón-Maiques, I.Fita, and V.Rubio (1999).
The carbamoyl-phosphate synthetase of Pyrococcus furiosus is enzymologically and structurally a carbamate kinase.
  J Biol Chem, 274, 16295-16303.  
10089364 T.M.Weaver, W.Wang, and S.E.Ealick (1999).
Purification, crystallization and preliminary X-ray diffraction data from selenomethionine glycinamide ribonucleotide synthetase.
  Acta Crystallogr D Biol Crystallogr, 55, 518-521.  
9478969 B.Mukhopadhyay, S.F.Stoddard, and R.S.Wolfe (1998).
Purification, regulation, and molecular and biochemical characterization of pyruvate carboxylase from Methanobacterium thermoautotrophicum strain deltaH.
  J Biol Chem, 273, 5155-5166.  
9668099 C.Z.Blanchard, and G.L.Waldrop (1998).
Overexpression and kinetic characterization of the carboxyltransferase component of acetyl-CoA carboxylase.
  J Biol Chem, 273, 19140-19145.  
9818189 F.M.Raushel, J.B.Thoden, G.D.Reinhart, and H.M.Holden (1998).
Carbamoyl phosphate synthetase: a crooked path from substrates to products.
  Curr Opin Chem Biol, 2, 624-632.  
9665735 F.M.Raushel, L.S.Mullins, and G.E.Gibson (1998).
A stringent test for the nucleotide switch mechanism of carbamoyl phosphate synthetase.
  Biochemistry, 37, 10272-10278.  
9914247 H.M.Holden, J.B.Thoden, and F.M.Raushel (1998).
Carbamoyl phosphate synthetase: a tunnel runs through it.
  Curr Opin Struct Biol, 8, 679-685.  
9597748 J.C.Wallace, S.Jitrapakdee, and A.Chapman-Smith (1998).
Pyruvate carboxylase.
  Int J Biochem Cell Biol, 30, 1-5.  
  10082373 K.A.Denessiouk, J.V.Lehtonen, and M.S.Johnson (1998).
Enzyme-mononucleotide interactions: three different folds share common structural elements for ATP recognition.
  Protein Sci, 7, 1768-1771.  
  9605318 K.A.Denessiouk, J.V.Lehtonen, T.Korpela, and M.S.Johnson (1998).
Two "unrelated" families of ATP-dependent enzymes share extensive structural similarities about their cofactor binding sites.
  Protein Sci, 7, 1136-1146.  
9463376 L.Esser, C.R.Wang, M.Hosaka, C.S.Smagula, T.C.Südhof, and J.Deisenhofer (1998).
Synapsin I is structurally similar to ATP-utilizing enzymes.
  EMBO J, 17, 977-984.
PDB codes: 1auv 1aux
9538689 O.Dideberg, and J.Bertrand (1998).
Tubulin tyrosine ligase: a shared fold with the glutathione synthetase ADP-forming family.
  Trends Biochem Sci, 23, 57-58.  
9551557 V.M.Levdikov, V.V.Barynin, A.I.Grebenko, W.R.Melik-Adamyan, V.S.Lamzin, and K.S.Wilson (1998).
The structure of SAICAR synthase: an enzyme in the de novo pathway of purine nucleotide biosynthesis.
  Structure, 6, 363-376.
PDB code: 1a48
9843369 W.Wang, T.J.Kappock, J.Stubbe, and S.E.Ealick (1998).
X-ray crystal structure of glycinamide ribonucleotide synthetase from Escherichia coli.
  Biochemistry, 37, 15647-15662.
PDB code: 1gso
9174345 J.B.Thoden, H.M.Holden, G.Wesenberg, F.M.Raushel, and I.Rayment (1997).
Structure of carbamoyl phosphate synthetase: a journey of 96 A from substrate to product.
  Biochemistry, 36, 6305-6316.  
9356452 M.Kothe, B.Eroglu, H.Mazza, H.Samudera, and S.Powers-Lee (1997).
Novel mechanism for carbamoyl-phosphate synthetase: a nucleotide switch for functionally equivalent domains.
  Proc Natl Acad Sci U S A, 94, 12348-12353.  
  9416615 M.Y.Galperin, and E.V.Koonin (1997).
A diverse superfamily of enzymes with ATP-dependent carboxylate-amine/thiol ligase activity.
  Protein Sci, 6, 2639-2643.  
8989312 N.Kobayashi, and N.Go (1997).
ATP binding proteins with different folds share a common ATP-binding structural motif.
  Nat Struct Biol, 4, 6-7.  
9398236 X.Yao, D.Wei, C.Soden, M.F.Summers, and D.Beckett (1997).
Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase.
  Biochemistry, 36, 15089-15100.
PDB code: 1a6x
8804825 A.G.Murzin (1996).
Structural classification of proteins: new superfamilies.
  Curr Opin Struct Biol, 6, 386-394.  
8695652 C.O.Rock, and J.E.Cronan (1996).
Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis.
  Biochim Biophys Acta, 1302, 1.  
8916923 F.Javid-Majd, M.A.Stapleton, M.F.Harmon, B.A.Hanks, L.S.Mullins, and F.M.Raushel (1996).
Comparison of the functional differences for the homologous residues within the carboxy phosphate and carbamate domains of carbamoyl phosphate synthetase.
  Biochemistry, 35, 14362-14369.  
8916922 M.A.Stapleton, F.Javid-Majd, M.F.Harmon, B.A.Hanks, J.L.Grahmann, L.S.Mullins, and F.M.Raushel (1996).
Role of conserved residues within the carboxy phosphate domain of carbamoyl phosphate synthetase.
  Biochemistry, 35, 14352-14361.  
8564538 P.J.Artymiuk, A.R.Poirrette, D.W.Rice, and P.Willett (1996).
Biotin carboxylase comes into the fold.
  Nat Struct Biol, 3, 128-132.  
8994880 Y.Lindqvist, and G.Schneider (1996).
Protein-biotin interactions.
  Curr Opin Struct Biol, 6, 798-803.  
7744060 E.Alonso, and V.Rubio (1995).
Affinity cleavage of carbamoyl-phosphate synthetase I localizes regions of the enzyme interacting with the molecule of ATP that phosphorylates carbamate.
  Eur J Biochem, 229, 377-384.  
8747466 F.K.Athappilly, and W.A.Hendrickson (1995).
Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing.
  Structure, 3, 1407-1419.
PDB code: 1bdo
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.