spacer
spacer

PDBsum entry 1bbp

Go to PDB code: 
protein ligands Protein-protein interface(s) links
Bilin binding PDB id
1bbp

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
173 a.a. *
Ligands
BLV ×4
Waters ×424
* Residue conservation analysis
PDB id:
1bbp
Name: Bilin binding
Title: Molecular structure of the bilin binding protein (bbp) from pieris brassicae after refinement at 2.0 angstroms resolution.
Structure: Bilin binding protein. Chain: a, b, c, d. Engineered: yes
Source: Pieris brassicae. Large cabbage white. Organism_taxid: 7116
Biol. unit: Tetramer (from PQS)
Resolution:
2.00Å     R-factor:   0.200    
Authors: R.Huber,M.Schneider,I.Mayr,R.Mueller,R.Deutzmann,F.Suter,H.Zuber, H.Falk,H.Kayser
Key ref: R.Huber et al. (1987). Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 A resolution. J Mol Biol, 198, 499-513. PubMed id: 3430616
Date:
19-Sep-90     Release date:   15-Oct-91    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
P09464  (BBP_PIEBR) -  Bilin-binding protein from Pieris brassicae
Seq:
Struc:
189 a.a.
173 a.a.
Key:    Secondary structure  CATH domain

 

 
J Mol Biol 198:499-513 (1987)
PubMed id: 3430616  
 
 
Molecular structure of the bilin binding protein (BBP) from Pieris brassicae after refinement at 2.0 A resolution.
R.Huber, M.Schneider, I.Mayr, R.Müller, R.Deutzmann, F.Suter, H.Zuber, H.Falk, H.Kayser.
 
  ABSTRACT  
 
The bilin binding protein (BBP) from the insect Pieris brassicae has been analysed for amino acid sequence, spectral properties and three-dimensional structure. The crystal structure that had been determined by isomorphous replacement has been refined at 2.0 A (1 A = 0.1 nm) resolution to an R-value of 0.20. The asymmetric unit contains four independent subunits of BBP. The co-ordinate differences are 0.25 A, in accord with the estimated error in co-ordinates. The polypeptide chain fold is characterized by an eight-stranded barrel. The connecting loops splay out at the upper end of the barrel and open it, whilst the lower end is closed. The overall shape resembles a calyx. The biliverdin IX gamma chromophore is located in a central cleft at the upper end of the barrel. The bilatriene moiety is in cyclic helical geometry with configuration Z,Z,Z and conformation syn,syn,syn. The geometry is in accord with the spectral properties and permits a correlation between sign of the circular dichroism bands and sense of the bilatriene helices. The fold of BBP is related to retinol binding protein (RBP), as had been recognized in the preliminary analysis, although the amino acid sequences of RBP and BBP show only 10% homology. There are large differences in the loops at the upper end of the barrel, whilst the segments of the centre and the lower end of the barrel superimpose closely. The ligands of BBP and RBP, biliverdin and retinol, respectively, are also similarly located.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19603796 J.L.Mills, G.Liu, A.Skerra, and T.Szyperski (2009).
NMR structure and dynamics of the engineered fluorescein-binding lipocalin FluA reveal rigidification of beta-barrel and variable loops upon enthalpy-driven ligand binding.
  Biochemistry, 48, 7411-7419.
PDB code: 1t0v
19864423 M.Kupka, J.Zhang, W.L.Fu, J.M.Tu, S.Böhm, P.Su, Y.Chen, M.Zhou, H.Scheer, and K.H.Zhao (2009).
Catalytic mechanism of S-type phycobiliprotein lyase: chaperone-like action and functional amino acid residues.
  J Biol Chem, 284, 36405-36414.  
19056737 Y.W.Tan, S.L.Chan, T.C.Ong, l.e. .Y.Yit, Y.S.Tiong, F.T.Chew, J.Sivaraman, and Y.K.Mok (2009).
Structures of Two Major Allergens, Bla g 4 and Per a 4, from Cockroaches and Their IgE Binding Epitopes.
  J Biol Chem, 284, 3148-3157.
PDB codes: 3ebk 3ebw
18435758 A.Skerra (2008).
Alternative binding proteins: anticalins - harnessing the structural plasticity of the lipocalin ligand pocket to engineer novel binding activities.
  FEBS J, 275, 2677-2683.  
18549244 N.C.Rockwell, S.L.Njuguna, L.Roberts, E.Castillo, V.L.Parson, S.Dwojak, J.C.Lagarias, and S.C.Spiller (2008).
A second conserved GAF domain cysteine is required for the blue/green photoreversibility of cyanobacteriochrome Tlr0924 from Thermosynechococcus elongatus.
  Biochemistry, 47, 7304-7316.  
18712529 R.Futahashi, and H.Fujiwara (2008).
Identification of stage-specific larval camouflage associated genes in the swallowtail butterfly, Papilio xuthus.
  Dev Genes Evol, 218, 491-504.  
17699160 A.Eichinger, A.Nasreen, H.J.Kim, and A.Skerra (2007).
Structural insight into the dual ligand specificity and mode of high density lipoprotein association of apolipoprotein D.
  J Biol Chem, 282, 31068-31075.
PDB codes: 2hzq 2hzr
16322568 A.Nasreen, M.Vogt, H.J.Kim, A.Eichinger, and A.Skerra (2006).
Solubility engineering and crystallization of human apolipoprotein D.
  Protein Sci, 15, 190-199.  
16552770 C.W.Choi, K.P.Nam, D.H.Seo, J.W.Choi, C.S.Lee, H.R.Kim, and C.Y.Yun (2006).
Comparative analysis of two biliproteins, BP1 and BP2, from haemolymph of cabbage white butterfly, Pieris rapae.
  Arch Insect Biochem Physiol, 61, 220-230.  
16360950 H.J.Kim, C.Y.Yun, Y.S.Han, I.H.Lee, Y.J.Kang, B.R.Jin, and S.J.Seo (2006).
cDNA sequences of two biliproteins, BP1 and BP2, from the cabbage white butterfly, Pieris rapae and their tissue- and stage-specific accumulation.
  Insect Biochem Mol Biol, 36, 54-62.  
16463267 Y.Yamada, K.Nakagawa, T.Yajima, K.Saito, A.Tokushima, K.Fujiwara, and M.Ikeguchi (2006).
Structural and thermodynamic consequences of removal of a conserved disulfide bond from equine beta-lactoglobulin.
  Proteins, 63, 595-602.  
16102419 H.J.Kim, H.J.Je, H.M.Cheon, S.Y.Kong, J.Han, C.Y.Yun, Y.S.Han, I.H.Lee, Y.J.Kang, and S.J.Seo (2005).
Accumulation of 23 kDa lipocalin during brain development and injury in Hyphantria cunea.
  Insect Biochem Mol Biol, 35, 1133-1141.  
15681226 H.Kayser, U.Krull-Savage, and R.Rilk-van Gessel (2005).
Developmental profiles of 5-aminolevulinate, porphobilinogen and porphobilinogen synthase activity in Pieris brassicae related to the synthesis of the bilin-binding protein.
  Insect Biochem Mol Biol, 35, 165-174.  
15665092 L.W.Schultz, L.Liu, M.Cegielski, and J.W.Hastings (2005).
Crystal structure of a pH-regulated luciferase catalyzing the bioluminescent oxidation of an open tetrapyrrole.
  Proc Natl Acad Sci U S A, 102, 1378-1383.
PDB code: 1vpr
15683711 M.Allhorn, A.Klapyta, and B.Akerström (2005).
Redox properties of the lipocalin alpha1-microglobulin: reduction of cytochrome c, hemoglobin, and free iron.
  Free Radic Biol Med, 38, 557-567.  
16207069 S.Schlehuber, and A.Skerra (2005).
Anticalins in drug development.
  BioDrugs, 19, 279-288.  
16255649 S.Schlehuber, and A.Skerra (2005).
Anticalins as an alternative to antibody technology.
  Expert Opin Biol Ther, 5, 1453-1462.  
16307475 S.Vopel, H.Mühlbach, and A.Skerra (2005).
Rational engineering of a fluorescein-binding anticalin for improved ligand affinity.
  Biol Chem, 386, 1097-1104.  
14760740 M.Vogt, and A.Skerra (2004).
Construction of an artificial receptor protein ("anticalin") based on the human apolipoprotein D.
  Chembiochem, 5, 191-199.  
14622015 B.Borucki, H.Otto, G.Rottwinkel, J.Hughes, M.P.Heyn, and T.Lamparter (2003).
Mechanism of Cph1 phytochrome assembly from stopped-flow kinetics and circular dichroism.
  Biochemistry, 42, 13684-13697.  
12945055 I.P.Korndörfer, G.Beste, and A.Skerra (2003).
Crystallographic analysis of an "anticalin" with tailored specificity for fluorescein reveals high structural plasticity of the lipocalin loop region.
  Proteins, 53, 121-129.
PDB code: 1n0s
11316880 D.E.Timm, L.J.Baker, H.Mueller, L.Zidek, and M.V.Novotny (2001).
Structural basis of pheromone binding to mouse major urinary protein (MUP-I).
  Protein Sci, 10, 997.
PDB codes: 1i04 1i05 1i06
11526314 E.J.Gordon, G.A.Leonard, S.McSweeney, and P.F.Zagalsky (2001).
The C1 subunit of alpha-crustacyanin: the de novo phasing of the crystal structure of a 40 kDa homodimeric protein using the anomalous scattering from S atoms combined with direct methods.
  Acta Crystallogr D Biol Crystallogr, 57, 1230-1237.
PDB code: 1i4u
11604536 L.H.Greene, E.D.Chrysina, L.I.Irons, A.C.Papageorgiou, K.R.Acharya, and K.Brew (2001).
Role of conserved residues in structure and stability: tryptophans of human serum retinol-binding protein, a model for the lipocalin superfamily.
  Protein Sci, 10, 2301-2316.
PDB codes: 1jyd 1jyj
11526313 M.Cianci, P.J.Rizkallah, A.Olczak, J.Raftery, N.E.Chayen, P.F.Zagalsky, and J.R.Helliwell (2001).
Structure of lobster apocrustacyanin A1 using softer X-rays.
  Acta Crystallogr D Biol Crystallogr, 57, 1219-1229.
PDB code: 1h91
11058774 A.Skerra (2000).
Lipocalins as a scaffold.
  Biochim Biophys Acta, 1482, 337-350.  
11058743 D.R.Flower, A.C.North, and C.E.Sansom (2000).
The lipocalin protein family: structural and sequence overview.
  Biochim Biophys Acta, 1482, 9.  
11058746 D.R.Flower (2000).
Experimentally determined lipocalin structures.
  Biochim Biophys Acta, 1482, 46-56.  
11048945 G.A.Weiss, and H.B.Lowman (2000).
Anticalins versus antibodies: made-to-order binding proteins for small molecules.
  Chem Biol, 7, R177-R184.  
  10716184 O.K.Gasymov, A.R.Abduragimov, T.N.Yusifov, and B.J.Glasgow (2000).
Resolution of ligand positions by site-directed tryptophan fluorescence in tear lipocalin.
  Protein Sci, 9, 325-331.  
11058749 R.E.Bishop (2000).
The bacterial lipocalins.
  Biochim Biophys Acta, 1482, 73-83.  
10736155 S.Uhrínová, M.H.Smith, G.B.Jameson, D.Uhrín, L.Sawyer, and P.N.Barlow (2000).
Structural changes accompanying pH-induced dissociation of the beta-lactoglobulin dimer.
  Biochemistry, 39, 3565-3574.
PDB code: 1dv9
10051566 G.Beste, F.S.Schmidt, T.Stibora, and A.Skerra (1999).
Small antibody-like proteins with prescribed ligand specificities derived from the lipocalin fold.
  Proc Natl Acad Sci U S A, 96, 1898-1903.  
9546222 A.Weichsel, J.F.Andersen, D.E.Champagne, F.A.Walker, and W.R.Montfort (1998).
Crystal structures of a nitric oxide transport protein from a blood-sucking insect.
  Nat Struct Biol, 5, 304-309.
PDB codes: 1np1 2np1 3np1
9485367 B.J.Glasgow, A.R.Abduragimov, T.N.Yusifov, O.K.Gasymov, J.Horwitz, W.L.Hubbell, and K.F.Faull (1998).
A conserved disulfide motif in human tear lipocalins influences ligand binding.
  Biochemistry, 37, 2215-2225.  
9887515 H.Saito (1998).
Purification and properties of two blue biliproteins from the larval hemolymph and integument of Rhodinia fugax (Lepidoptera: Saturniidae).
  Insect Biochem Mol Biol, 28, 995.  
9853680 H.Santa, J.T.Saarela, R.Laatikainen, J.Rautianen, T.Virtanen, M.Rytkönen, and R.Mäntyjärvi (1998).
A bovine dander allergen, comparative modeling, and similarities and differences in folding with related proteins.
  J Protein Chem, 17, 657-662.  
9782054 J.F.Andersen, A.Weichsel, C.A.Balfour, D.E.Champagne, and W.R.Montfort (1998).
The crystal structure of nitrophorin 4 at 1.5 A resolution: transport of nitric oxide by a lipocalin-based heme protein.
  Structure, 6, 1315-1327.
PDB code: 1np4
9669522 J.J.Lareyre, M.G.Mattéi, S.Kasper, D.E.Ong, R.J.Matusik, and M.C.Orgebin-Crist (1998).
Genomic organization and chromosomal localization of the murine epididymal retinoic acid-binding protein (mE-RABP) gene.
  Mol Reprod Dev, 50, 387-395.  
9624110 R.C.Bugos, A.D.Hieber, and H.Y.Yamamoto (1998).
Xanthophyll cycle enzymes are members of the lipocalin family, the first identified from plants.
  J Biol Chem, 273, 15321-15324.  
9342325 P.Fuentes-Prior, C.Noeske-Jungblut, P.Donner, W.D.Schleuning, R.Huber, and W.Bode (1997).
Structure of the thrombin complex with triabin, a lipocalin-like exosite-binding inhibitor derived from a triatomine bug.
  Proc Natl Acad Sci U S A, 94, 11845-11850.
PDB code: 1avg
9115437 S.Brownlow, J.H.Morais Cabral, R.Cooper, D.R.Flower, S.J.Yewdall, I.Polikarpov, A.C.North, and L.Sawyer (1997).
Bovine beta-lactoglobulin at 1.8 A resolution--still an enigmatic lipocalin.
  Structure, 5, 481-495.
PDB code: 1beb
  8819158 G.Lepperdinger, B.Strobl, A.Jilek, A.Weber, J.Thalhamer, H.Flöckner, and C.Mollay (1996).
The lipocalin Xlcpl1 expressed in the neural plate of Xenopus laevis embryos is a secreted retinaldehyde binding protein.
  Protein Sci, 5, 1250-1260.  
8727319 G.V.Louie, P.D.Brownlie, R.Lambert, J.B.Cooper, T.L.Blundell, S.P.Wood, V.N.Malashkevich, A.Hädener, M.J.Warren, and P.M.Shoolingin-Jordan (1996).
The three-dimensional structure of Escherichia coli porphobilinogen deaminase at 1.76-A resolution.
  Proteins, 25, 48-78.  
8901871 M.A.Bianchet, G.Bains, P.Pelosi, J.Pevsner, S.H.Snyder, H.L.Monaco, and L.M.Amzel (1996).
The three-dimensional structure of bovine odorant binding protein and its mechanism of odor recognition.
  Nat Struct Biol, 3, 934-939.
PDB code: 1pbo
8701467 R.E.Bishop, and J.H.Weiner (1996).
"Outlier' lipocalins more than peripheral.
  Trends Biochem Sci, 21, 127.  
8573354 D.R.Flower (1995).
Multiple molecular recognition properties of the lipocalin protein family.
  J Mol Recognit, 8, 185-195.  
7559452 R.E.Bishop, S.S.Penfold, L.S.Frost, J.V.Höltje, and J.H.Weiner (1995).
Stationary phase expression of a novel Escherichia coli outer membrane lipoprotein and its relationship with mammalian apolipoprotein D. Implications for the origin of lipocalins.
  J Biol Chem, 270, 23097-23103.  
  8069218 C.Daffner, G.Chelvanayagam, and P.Argos (1994).
Structural characteristics and stabilizing principles of bent beta-strands in protein tertiary architectures.
  Protein Sci, 3, 876-882.  
8112337 F.S.Schmidt, and A.Skerra (1994).
The bilin-binding protein of Pieris brassicae. cDNA sequence and regulation of expression reveal distinct features of this insect pigment protein.
  Eur J Biochem, 219, 855-863.  
7514123 K.Kock, C.Ahlers, and H.Schmale (1994).
Structural organization of the genes for rat von Ebner's gland proteins 1 and 2 reveals their close relationship to lipocalins.
  Eur J Biochem, 221, 905-916.  
  8069217 N.N.Alexandrov, and N.Go (1994).
Biological meaning, statistical significance, and classification of local spatial similarities in nonhomologous proteins.
  Protein Sci, 3, 866-875.  
7876898 P.L.Chau, and P.M.Dean (1994).
Electrostatic complementarity between proteins and ligands. 1. Charge disposition, dielectric and interface effects.
  J Comput Aided Mol Des, 8, 513-525.  
7876899 P.L.Chau, and P.M.Dean (1994).
Electrostatic complementarity between proteins and ligands. 2. Ligand moieties.
  J Comput Aided Mol Des, 8, 527-544.  
  7684291 D.R.Flower, A.C.North, and T.K.Attwood (1993).
Structure and sequence relationships in the lipocalins and related proteins.
  Protein Sci, 2, 753-761.  
1623143 H.L.Monaco, and G.Zanotti (1992).
Three-dimensional structure and active site of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity.
  Biopolymers, 32, 457-465.  
1572353 W.Li, and L.M.Riddiford (1992).
Two distinct genes encode two major isoelectric forms of insecticyanin in the tobacco hornworm, Manduca sexta.
  Eur J Biochem, 205, 491-499.  
1935978 J.N.Keen, I.Caceres, E.E.Eliopoulos, P.F.Zagalsky, and J.B.Findlay (1991).
Complete sequence and model for the C1 subunit of the carotenoprotein, crustacyanin, and model for the dimer, beta-crustacyanin, formed from the C1 and A2 subunits with astaxanthin.
  Eur J Biochem, 202, 31-40.  
2026162 J.N.Keen, I.Caceres, E.E.Eliopoulos, P.F.Zagalsky, and J.B.Findlay (1991).
Complete sequence and model for the A2 subunit of the carotenoid pigment complex, crustacyanin.
  Eur J Biochem, 197, 407-417.  
1881879 R.Lüthy, A.D.McLachlan, and D.Eisenberg (1991).
Secondary structure-based profiles: use of structure-conserving scoring tables in searching protein sequence databases for structural similarities.
  Proteins, 10, 229-239.  
2226471 H.Marko, N.Müller, and H.Falk (1990).
Nuclear-magnetic-resonance investigations of the biliverdin-apomyoglobin complex.
  Eur J Biochem, 193, 573-580.  
2404762 R.Huber (1990).
E. Antonini Plenary lecture. A structural basis of light energy and electron transfer in biology.
  Eur J Biochem, 187, 283-305.  
2217163 S.W.Cowan, M.E.Newcomer, and T.A.Jones (1990).
Crystallographic refinement of human serum retinol binding protein at 2A resolution.
  Proteins, 8, 44-61.
PDB code: 1rbp
2771940 D.E.McRee, J.A.Tainer, T.E.Meyer, J.Van Beeumen, M.A.Cusanovich, and E.D.Getzoff (1989).
Crystallographic structure of a photoreceptor protein at 2.4 A resolution.
  Proc Natl Acad Sci U S A, 86, 6533-6537.
PDB code: 1phy
2682622 J.C.Sacchettini, J.I.Gordon, and L.J.Banaszak (1989).
Refined apoprotein structure of rat intestinal fatty acid binding protein produced in Escherichia coli.
  Proc Natl Acad Sci U S A, 86, 7736-7740.
PDB code: 1ifb
2692721 R.Huber (1989).
Nobel lecture. A structural basis of light energy and electron transfer in biology.
  Biosci Rep, 9, 635-673.  
  2676513 R.Huber (1989).
Nobel lecture. A structural basis of light energy and electron transfer in biology.
  EMBO J, 8, 2125-2147.  
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.

 

spacer

spacer