PDBsum entry 1bib

Go to PDB code: 
protein ligands links
Transcription regulation PDB id
Protein chain
294 a.a. *
Waters ×19
* Residue conservation analysis
PDB id:
Name: Transcription regulation
Title: The e. Coli biotin holoenzyme synthetase(slash)bio repressor crystal structure delineates the biotin and DNA- binding domains
Structure: Bir a. Chain: a. Engineered: yes
Source: Escherichia coli. Organism_taxid: 562
2.80Å     R-factor:   0.173    
Authors: K.P.Wilson,L.M.Shewchuk,B.W.Matthews
Key ref: K.P.Wilson et al. (1992). Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains. Proc Natl Acad Sci U S A, 89, 9257-9261. PubMed id: 1409631 DOI: 10.1073/pnas.89.19.9257
06-Jul-92     Release date:   31-Oct-93    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P06709  (BIRA_ECOLI) -  Bifunctional ligase/repressor BirA
321 a.a.
294 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.  - Biotin--[acetyl-CoA-carboxylase] ligase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + biotin + apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
Bound ligand (Het Group name = BTN)
corresponds exactly
+ apo-[acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
+ diphosphate
+ [acetyl-CoA:carbon-dioxide ligase (ADP-forming)]
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     biotin biosynthetic process   5 terms 
  Biochemical function     nucleotide binding     5 terms  


DOI no: 10.1073/pnas.89.19.9257 Proc Natl Acad Sci U S A 89:9257-9261 (1992)
PubMed id: 1409631  
Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.
K.P.Wilson, L.M.Shewchuk, R.G.Brennan, A.J.Otsuka, B.W.Matthews.
The three-dimensional structure of BirA, the repressor of the Escherichia coli biotin biosynthetic operon, has been determined by x-ray crystallography and refined to a crystallographic residual of 19.0% at 2.3-A resolution. BirA is a sequence-specific DNA-binding protein that also catalyzes the formation of biotinyl-5'-adenylate from biotin and ATP and transfers the biotin moiety to other proteins. The level of biotin biosynthetic enzymes in the cell is controlled by the amount of biotinyl-5'-adenylate, which is the BirA corepressor. The structure provides an example of a transcription factor that is also an enzyme. The structure of BirA is highly asymmetric and consists of three domains. The N-terminal domain is mostly alpha-helical, contains a helix-turn-helix DNA-binding motif, and is loosely connected to the remainder of the molecule. The central domain consists of a seven-stranded mixed beta-sheet with alpha-helices covering one face. The other side of the sheet is largely solvent-exposed and contains the active site. The C-terminal domain comprises a six-stranded, antiparallel beta-sheet sandwich. The location of biotin binding is consistent with mutations that affect enzymatic activity. A nearby loop has a sequence that has been associated with phosphate binding in other proteins. It is inferred that ATP binds in this region, adjacent to the biotin. It is proposed that the binding of corepressor to monomeric BirA may promote DNA binding by facilitating the formation of a multimeric BirA-corepressor-DNA complex. The structural details of this complex remain an open question, however.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20970983 D.Men, Z.P.Zhang, Y.C.Guo, D.H.Zhu, L.J.Bi, J.Y.Deng, Z.Q.Cui, H.P.Wei, and X.E.Zhang (2010).
An auto-biotinylated bifunctional protein nanowire for ultra-sensitive molecular biosensing.
  Biosens Bioelectron, 26, 1137-1141.  
20089862 K.Fujiwara, N.Maita, H.Hosaka, K.Okamura-Ikeda, A.Nakagawa, and H.Taniguchi (2010).
Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A.
  J Biol Chem, 285, 9971-9980.
PDB codes: 3a7a 3a7l 3a7r 3a7u
20169168 V.Gupta, R.K.Gupta, G.Khare, D.M.Salunke, A.Surolia, and A.K.Tyagi (2010).
Structural ordering of disordered ligand-binding loops of biotin protein ligase into active conformations as a consequence of dehydration.
  PLoS One, 5, e9222.
PDB codes: 3l1a 3l2z
20622127 Y.Maeda, T.Yoshino, and T.Matsunaga (2010).
In vivo biotinylation of bacterial magnetic particles by a truncated form of Escherichia coli biotin ligase and biotin acceptor peptide.
  Appl Environ Microbiol, 76, 5785-5790.  
  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.  
19184528 R.Janowski, S.Panjikar, A.N.Eddine, S.H.Kaufmann, and M.S.Weiss (2009).
Structural analysis reveals DNA binding properties of Rv2827c, a hypothetical protein from Mycobacterium tuberculosis.
  J Struct Funct Genomics, 10, 137-150.
PDB code: 1zel
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.  
18353365 C.J.Tsai, A.del Sol, and R.Nussinov (2008).
Allostery: absence of a change in shape does not imply that allostery is not at play.
  J Mol Biol, 378, 1.  
18812514 J.Meisner, X.Wang, M.Serrano, A.O.Henriques, and C.P.Moran (2008).
A channel connecting the mother cell and forespore during bacterial endospore formation.
  Proc Natl Acad Sci U S A, 105, 15100-15105.  
  18540065 N.R.Pendini, S.W.Polyak, G.W.Booker, J.C.Wallace, and M.C.Wilce (2008).
Purification, crystallization and preliminary crystallographic analysis of biotin protein ligase from Staphylococcus aureus.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 64, 520-523.  
18586268 O.Laine, E.D.Streaker, M.Nabavi, C.C.Fenselau, and D.Beckett (2008).
Allosteric signaling in the biotin repressor occurs via local folding coupled to global dampening of protein dynamics.
  J Mol Biol, 381, 89.  
18509457 S.Purushothaman, G.Gupta, R.Srivastava, V.G.Ramu, and A.Surolia (2008).
Ligand specificity of group I biotin protein ligase of Mycobacterium tuberculosis.
  PLoS ONE, 3, e2320.  
17669049 D.Beckett (2007).
Biotin sensing: universal influence of biotin status on transcription.
  Annu Rev Genet, 41, 443-464.  
17123129 M.Iro, R.Klein, B.Gálos, U.Baranyi, N.Rössler, and A.Witte (2007).
The lysogenic region of virus phiCh1: identification of a repressor-operator system and determination of its activity in halophilic Archaea.
  Extremophiles, 11, 383-396.  
17765263 S.Naganathan, and D.Beckett (2007).
Nucleation of an allosteric response via ligand-induced loop folding.
  J Mol Biol, 373, 96.  
16735476 Q.Ma, X.Zhao, A.Nasser Eddine, A.Geerlof, X.Li, J.E.Cronan, S.H.Kaufmann, and M.Wilmanns (2006).
The Mycobacterium tuberculosis LipB enzyme functions as a cysteine/lysine dyad acyltransferase.
  Proc Natl Acad Sci U S A, 103, 8662-8667.
PDB code: 1w66
  16510991 B.Bagautdinov, C.Kuroishi, M.Sugahara, and N.Kunishima (2005).
Purification, crystallization and preliminary crystallographic analysis of the biotin-protein ligase from Pyrococcus horikoshii OT3.
  Acta Crystallogr Sect F Struct Biol Cryst Commun, 61, 193-195.  
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.  
15808743 L.Aravind, V.Anantharaman, S.Balaji, M.M.Babu, and L.M.Iyer (2005).
The many faces of the helix-turn-helix domain: transcription regulation and beyond.
  FEMS Microbiol Rev, 29, 231-262.  
15562516 N.Rekha, S.M.Machado, C.Narayanan, A.Krupa, and N.Srinivasan (2005).
Interaction interfaces of protein domains are not topologically equivalent across families within superfamilies: Implications for metabolic and signaling pathways.
  Proteins, 58, 339-353.  
15678423 S.Fujita, T.Taki, and K.Taira (2005).
Selection of an active enzyme by phage display on the basis of the enzyme's catalytic activity in vivo.
  Chembiochem, 6, 315-321.  
  15623830 T.I.Vlasova, S.L.Stratton, A.M.Wells, N.I.Mock, and D.M.Mock (2005).
Biotin deficiency reduces expression of SLC19A3, a potential biotin transporter, in leukocytes from human blood.
  J Nutr, 135, 42-47.  
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.  
15449372 M.S.Lee, W.A.Joo, and C.W.Kim (2004).
Identification of a novel protein D3UPCA from Halobacterium salinarum and prediction of its function.
  Proteomics, 4, 3622-3631.  
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.  
12837782 J.A.D'Aquino, and D.Ringe (2003).
Determinants of the SRC homology domain 3-like fold.
  J Bacteriol, 185, 4081-4086.
PDB code: 1p92
12837783 S.C.Sinha, J.Krahn, B.S.Shin, D.R.Tomchick, H.Zalkin, and J.L.Smith (2003).
The purine repressor of Bacillus subtilis: a novel combination of domains adapted for transcription regulation.
  J Bacteriol, 185, 4087-4098.
PDB codes: 1o57 1p41
12124727 A.Morrone, S.Malvagia, M.A.Donati, S.Funghini, F.Ciani, I.Pela, A.Boneh, H.Peters, E.Pasquini, and E.Zammarchi (2002).
Clinical findings and biochemical and molecular analysis of four patients with holocarboxylase synthetase deficiency.
  Am J Med Genet, 111, 10-18.  
12458790 C.Francklyn, J.J.Perona, J.Puetz, and Y.M.Hou (2002).
Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation.
  RNA, 8, 1363-1372.  
11839496 J.L.Huffman, and R.G.Brennan (2002).
Prokaryotic transcription regulators: more than just the helix-turn-helix motif.
  Curr Opin Struct Biol, 12, 98.  
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.  
11714929 A.Chapman-Smith, T.D.Mulhern, F.Whelan, J.E.Cronan, and J.C.Wallace (2001).
The C-terminal domain of biotin protein ligase from E. coli is required for catalytic activity.
  Protein Sci, 10, 2608-2617.  
11371547 B.Mukhopadhyay, E.Purwantini, C.L.Kreder, and R.S.Wolfe (2001).
Oxaloacetate synthesis in the methanarchaeon Methanosarcina barkeri: pyruvate carboxylase genes and a putative Escherichia coli-type bifunctional biotin protein ligase gene (bpl/birA) exhibit a unique organization.
  J Bacteriol, 183, 3804-3810.  
11353844 L.H.Weaver, K.Kwon, D.Beckett, and B.W.Matthews (2001).
Corepressor-induced organization and assembly of the biotin repressor: a model for allosteric activation of a transcriptional regulator.
  Proc Natl Acad Sci U S A, 98, 6045-6050.
PDB code: 1hxd
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
15012185 C.Alban, D.Job, and R.Douce (2000).
  Annu Rev Plant Physiol Plant Mol Biol, 51, 17-47.  
10734204 E.Pérez-Rueda, and J.Collado-Vides (2000).
The repertoire of DNA-binding transcriptional regulators in Escherichia coli K-12.
  Nucleic Acids Res, 28, 1838-1847.  
  10975574 K.Kwon, and D.Beckett (2000).
Function of a conserved sequence motif in biotin holoenzyme synthetases.
  Protein Sci, 9, 1530-1539.  
10679470 K.S.Gajiwala, and S.K.Burley (2000).
Winged helix proteins.
  Curr Opin Struct Biol, 10, 110-116.  
10716934 M.Okuda, Y.Watanabe, H.Okamura, F.Hanaoka, Y.Ohkuma, and Y.Nishimura (2000).
Structure of the central core domain of TFIIEbeta with a novel double-stranded DNA-binding surface.
  EMBO J, 19, 1346-1356.
PDB codes: 1d8j 1d8k
  11106165 P.A.Reche (2000).
Lipoylating and biotinylating enzymes contain a homologous catalytic module.
  Protein Sci, 9, 1922-1929.  
10966480 R.N.Perham (2000).
Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions.
  Annu Rev Biochem, 69, 961.  
10796994 A.Chapman-Smith, and J.E.Cronan (1999).
In vivo enzymatic protein biotinylation.
  Biomol Eng, 16, 119-125.  
10470036 A.Chapman-Smith, and J.E.Cronan (1999).
The enzymatic biotinylation of proteins: a post-translational modification of exceptional specificity.
  Trends Biochem Sci, 24, 359-363.  
10075918 A.Nakagawa, T.Nakashima, M.Taniguchi, H.Hosaka, M.Kimura, and I.Tanaka (1999).
The three-dimensional structure of the RNA-binding domain of ribosomal protein L2; a protein at the peptidyl transferase center of the ribosome.
  EMBO J, 18, 1459-1467.
PDB code: 1rl2
10450096 A.P.Eijkelenboom, R.Sprangers, K.Hård, R.A.Puras Lutzke, R.H.Plasterk, R.Boelens, and R.Kaptein (1999).
Refined solution structure of the C-terminal DNA-binding domain of human immunovirus-1 integrase.
  Proteins, 36, 556-564.
PDB code: 1qmc
  10211839 D.Beckett, E.Kovaleva, and P.J.Schatz (1999).
A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation.
  Protein Sci, 8, 921-929.  
10213607 E.L.Roberts, N.Shu, M.J.Howard, R.W.Broadhurst, A.Chapman-Smith, J.C.Wallace, T.Morris, J.E.Cronan, and R.N.Perham (1999).
Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy.
  Biochemistry, 38, 5045-5053.
PDB codes: 2bdo 3bdo
10500170 M.P.Morrissey, and E.I.Shakhnovich (1999).
Evidence for the role of PrP(C) helix 1 in the hydrophilic seeding of prion aggregates.
  Proc Natl Acad Sci U S A, 96, 11293-11298.  
10329614 P.Reche, and R.N.Perham (1999).
Structure and selectivity in post-translational modification: attaching the biotinyl-lysine and lipoyl-lysine swinging arms in multifunctional enzymes.
  EMBO J, 18, 2673-2682.  
  10368153 W.G.Voorhorst, Y.Gueguen, A.C.Geerling, G.Schut, I.Dahlke, M.Thomm, J.van der Oost, and Vos (1999).
Transcriptional regulation in the hyperthermophilic archaeon Pyrococcus furiosus: coordinated expression of divergently oriented genes in response to beta-linked glucose polymers.
  J Bacteriol, 181, 3777-3783.  
9689043 C.M.Groft, S.N.Uljon, R.Wang, and M.H.Werner (1998).
Structural homology between the Rap30 DNA-binding domain and linker histone H5: implications for preinitiation complex assembly.
  Proc Natl Acad Sci U S A, 95, 9117-9122.
PDB codes: 1bby 2bby
9485476 E.D.Streaker, and D.Beckett (1998).
Coupling of site-specific DNA binding to protein dimerization in assembly of the biotin repressor-biotin operator complex.
  Biochemistry, 37, 3210-3219.  
9562558 J.Furui, K.Uegaki, T.Yamazaki, M.Shirakawa, M.B.Swindells, H.Harada, T.Taniguchi, and Y.Kyogoku (1998).
Solution structure of the IRF-2 DNA-binding domain: a novel subgroup of the winged helix-turn-helix family.
  Structure, 6, 491-500.
PDB codes: 1irf 1irg
9565750 J.P.Schneider, A.Lombardi, and W.F.DeGrado (1998).
Analysis and design of three-stranded coiled coils and three-helix bundles.
  Fold Des, 3, R29-R40.  
9593201 S.Knapp, P.T.Mattson, P.Christova, K.D.Berndt, A.Karshikoff, M.Vihinen, C.I.Smith, and R.Ladenstein (1998).
Thermal unfolding of small proteins with SH3 domain folding pattern.
  Proteins, 31, 309-319.  
9530015 W.J.Wu, and D.P.Raleigh (1998).
Local control of peptide conformation: stabilization of cis proline peptide bonds by aromatic proline interactions.
  Biopolymers, 45, 381-394.  
9368756 A.P.Eijkelenboom, F.M.van den Ent, A.Vos, J.F.Doreleijers, K.Hård, T.D.Tullius, R.H.Plasterk, R.Kaptein, and R.Boelens (1997).
The solution structure of the amino-terminal HHCC domain of HIV-2 integrase: a three-helix bundle stabilized by zinc.
  Curr Biol, 7, 739-746.
PDB code: 1aub
9016718 E.Martínez-Hackert, and A.M.Stock (1997).
The DNA-binding domain of OmpR: crystal structures of a winged helix transcription factor.
  Structure, 5, 109-124.
PDB code: 1opc
8989318 H.Kondo, A.Nakagawa, J.Nishihira, Y.Nishimura, T.Mizuno, and I.Tanaka (1997).
Escherichia coli positive regulator OmpR has a large loop structure at the putative RNA polymerase interaction site.
  Nat Struct Biol, 4, 28-31.
PDB code: 1odd
  9144769 J.E.Gready, S.Ranganathan, P.R.Schofield, Y.Matsuo, and K.Nishikawa (1997).
Predicted structure of the extracellular region of ligand-gated ion-channel receptors shows SH2-like and SH3-like domains forming the ligand-binding site.
  Protein Sci, 6, 983-998.  
9032054 M.A.Kercher, P.Lu, and M.Lewis (1997).
Lac repressor-operator complex.
  Curr Opin Struct Biol, 7, 76-85.  
9334747 M.Sunnerhagen, M.Nilges, G.Otting, and J.Carey (1997).
Solution structure of the DNA-binding domain and model for the complex of multifunctional hexameric arginine repressor with DNA.
  Nat Struct Biol, 4, 819-826.
PDB code: 1aoy
9032065 S.K.Burley, X.Xie, K.L.Clark, and F.Shu (1997).
Histone-like transcription factors in eukaryotes.
  Curr Opin Struct Biol, 7, 94.  
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
9396568 Y.Aoki, Y.Suzuki, X.Li, O.Sakamoto, H.Chikaoka, S.Takita, and K.Narisawa (1997).
Characterization of mutant holocarboxylase synthetase (HCS): a Km for biotin was not elevated in a patient with HCS deficiency.
  Pediatr Res, 42, 849-854.  
8989317 Y.Xing, D.Guha Thakurta, and D.E.Draper (1997).
The RNA binding domain of ribosomal protein L11 is structurally similar to homeodomains.
  Nat Struct Biol, 4, 24-27.  
8805554 C.J.Morton, D.J.Pugh, E.L.Brown, J.D.Kahmann, D.A.Renzoni, and I.D.Campbell (1996).
Solution structure and peptide binding of the SH3 domain from human Fyn.
  Structure, 4, 705-714.
PDB codes: 1nyf 1nyg
8805533 E.Conti, N.P.Franks, and P.Brick (1996).
Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes.
  Structure, 4, 287-298.
PDB code: 1lci
8548458 J.J.Tesmer, T.J.Klem, M.L.Deras, V.J.Davisson, and J.L.Smith (1996).
The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families.
  Nat Struct Biol, 3, 74-86.
PDB code: 1gpm
8831284 K.van Holde, and J.Zlatanova (1996).
Chromatin architectural proteins and transcription factors: a structural connection.
  Bioessays, 18, 697-700.  
  8598195 L.W.Donaldson, J.M.Petersen, B.J.Graves, and L.P.McIntosh (1996).
Solution structure of the ETS domain from murine Ets-1: a winged helix-turn-helix DNA binding motif.
  EMBO J, 15, 125-134.
PDB codes: 1etc 1etd
8605176 P.Dumoulin, R.H.Ebright, R.Knegtel, R.Kaptein, M.Granger-Schnarr, and M.Schnarr (1996).
Structure of the LexA repressor-DNA complex probed by affinity cleavage and affinity photo-cross-linking.
  Biochemistry, 35, 4279-4286.  
8696976 P.Rice, R.Craigie, and D.R.Davies (1996).
Retroviral integrases and their cousins.
  Curr Opin Struct Biol, 6, 76-83.  
8823163 X.Qiu, E.Pohl, R.K.Holmes, and W.G.Hol (1996).
High-resolution structure of the diphtheria toxin repressor complexed with cobalt and manganese reveals an SH3-like third domain and suggests a possible role of phosphate as co-corepressor.
  Biochemistry, 35, 12292-12302.
PDB code: 2dtr
8994880 Y.Lindqvist, and G.Schneider (1996).
Protein-biotin interactions.
  Curr Opin Struct Biol, 6, 798-803.  
8611542 Y.Xu, C.R.Johnson, and D.Beckett (1996).
Thermodynamic analysis of small ligand binding to the Escherichia coli repressor of biotin biosynthesis.
  Biochemistry, 35, 5509-5517.  
8639659 Y.Xu, and D.Beckett (1996).
Evidence for interdomain interaction in the Escherichia coli repressor of biotin biosynthesis from studies of an N-terminal domain deletion mutant.
  Biochemistry, 35, 1783-1792.  
7753853 A.León-Del-Rio, D.Leclerc, B.Akerman, N.Wakamatsu, and R.A.Gravel (1995).
Isolation of a cDNA encoding human holocarboxylase synthetase by functional complementation of a biotin auxotroph of Escherichia coli.
  Proc Natl Acad Sci U S A, 92, 4626-4630.  
  7663343 A.S.Siddiqui, and G.J.Barton (1995).
Continuous and discontinuous domains: an algorithm for the automatic generation of reliable protein domain definitions.
  Protein Sci, 4, 872-884.  
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
  8563641 M.Safro, and L.Mosyak (1995).
Structural similarities in the noncatalytic domains of phenylalanyl-tRNA and biotin synthetases.
  Protein Sci, 4, 2429-2432.  
7568230 N.Schiering, X.Tao, H.Zeng, J.R.Murphy, G.A.Petsko, and D.Ringe (1995).
Structures of the apo- and the metal ion-activated forms of the diphtheria tox repressor from Corynebacterium diphtheriae.
  Proc Natl Acad Sci U S A, 92, 9843-9850.
PDB code: 1dpr
  7744010 R.Ficner, U.H.Sauer, G.Stier, and D.Suck (1995).
Three-dimensional structure of the bifunctional protein PCD/DCoH, a cytoplasmic enzyme interacting with transcription factor HNF1.
  EMBO J, 14, 2034-2042.  
  7730294 S.Bower, J.Perkins, R.R.Yocum, P.Serror, A.Sorokin, P.Rahaim, C.L.Howitt, N.Prasad, S.D.Ehrlich, and J.Pero (1995).
Cloning and characterization of the Bacillus subtilis birA gene encoding a repressor of the biotin operon.
  J Bacteriol, 177, 2572-2575.  
  7868594 S.L.Otten, J.Ferguson, and C.R.Hutchinson (1995).
Regulation of daunorubicin production in Streptomyces peucetius by the dnrR2 locus.
  J Bacteriol, 177, 1216-1224.  
8710828 T.Madej, J.F.Gibrat, and S.H.Bryant (1995).
Threading a database of protein cores.
  Proteins, 23, 356-369.  
7937731 L.Holm, and C.Sander (1994).
Searching protein structure databases has come of age.
  Proteins, 19, 165-173.  
  8076591 R.H.Fogh, G.Ottleben, H.Rüterjans, M.Schnarr, R.Boelens, and R.Kaptein (1994).
Solution structure of the LexA repressor DNA binding domain determined by 1H NMR spectroscopy.
  EMBO J, 13, 3936-3944.
PDB codes: 1lea 1leb
7881904 R.T.Clubb, J.G.Omichinski, H.Savilahti, K.Mizuuchi, A.M.Gronenborn, and G.M.Clore (1994).
A novel class of winged helix-turn-helix protein: the DNA-binding domain of Mu transposase.
  Structure, 2, 1041-1048.
PDB codes: 1tns 1tnt
  7687536 M.E.Noble, A.Musacchio, M.Saraste, S.A.Courtneidge, and R.K.Wierenga (1993).
Crystal structure of the SH3 domain in human Fyn; comparison of the three-dimensional structures of SH3 domains in tyrosine kinases and spectrin.
  EMBO J, 12, 2617-2624.
PDB code: 1shf
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.