scholarly journals Control of domain swapping in bovine odorant-binding protein

2002 ◽  
Vol 365 (3) ◽  
pp. 739-748 ◽  
Author(s):  
Roberto RAMONI ◽  
Florence VINCENT ◽  
Alison E. ASHCROFT ◽  
Paolo ACCORNERO ◽  
Stefano GROLLI ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Binding Protein ◽  
Odorant Binding Protein ◽  
Domain Swapping ◽  
Disulphide Bridge ◽  
Dimer Interface ◽  
X Ray ◽  
Glycine Residue ◽  
Α Helix ◽  
Odorant Binding

As revealed by the X-ray structure, bovine odorant-binding protein (OBPb) is a domain swapped dimer [Tegoni, Ramoni, Bignetti, Spinelli and Cambillau (1996) Nat. Struct. Biol. 3, 863–867; Bianchet, Bains, Petosi, Pevsner, Snyder, Monaco and Amzel (1996) Nat. Struct. Biol. 3, 934–939]. This contrasts with all known mammalian OBPs, which are monomers, and in particular with porcine OBP (OBPp), sharing 42.3% identity with OBPb. By the mechanism of domain swapping, monomers are proposed to evolve into dimers and oligomers, as observed in human prion. Comparison of bovine and porcine OBP sequences pointed at OBPp glycine 121, in the hinge linking the β-barrel to the α-helix. The absence of this residue in OBPb might explain why the normal lipocalin β-turn is not formed. In order to decipher the domain swapping determinants we have produced a mutant of OBPb in which a glycine residue was inserted after position 121, and a mutant of OBPp in which glycine 121 was deleted. The latter mutation did not result in dimerization, while OBPb-121Gly+ became monomeric, suggesting that domain swapping was reversed. Careful structural analysis revealed that besides the presence of a glycine in the hinge, the dimer interface formed by the C-termini and by the presence of the lipocalins conserved disulphide bridge may also control domain swapping.

Domain swapping creates a third putative combining site in bovine odorant binding protein dimer

1996 ◽  
Vol 3 (10) ◽  
pp. 863-867 ◽  
Author(s):  
Mariella Tegoni ◽  
Roberto Ramoni ◽  
Enrico Bignetti ◽  
Silvia Spinelli ◽  
Christian Cambillau
Keyword(s):  
Binding Protein ◽  
Odorant Binding Protein ◽  
Domain Swapping ◽  
Protein Dimer ◽  
Odorant Binding

The Structure of the Monomeric Porcine Odorant Binding Protein Sheds Light on the Domain Swapping Mechanism‡

Biochemistry ◽  
1998 ◽  
Vol 37 (22) ◽  
pp. 7913-7918 ◽  
Author(s):  
Silvia Spinelli ◽  
Roberto Ramoni ◽  
Stefano Grolli ◽  
Jacques Bonicel ◽  
Christian Cambillau ◽  
...  
Keyword(s):  
Binding Protein ◽  
Odorant Binding Protein ◽  
Domain Swapping ◽  
Odorant Binding ◽  
Porcine Odorant Binding Protein

scholarly journals Structure and stability of recombinant bovine odorant-binding protein: I. Design and analysis of monomeric mutants

2015 ◽  
Author(s):  
Olga V Stepanenko ◽  
Denis O Roginskii ◽  
Olesya V Stepanenko ◽  
Irina M Kuznetsova ◽  
Vladimir N Uversky ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Binding Protein ◽  
Stable State ◽  
Structural Features ◽  
Odorant Binding Protein ◽  
Domain Swapping ◽  
Tryptophan Residues ◽  
Monomeric Structure ◽  
Odorant Binding

Bovine odorant-binding protein (bOBP) differs from other lipocalins by lacking the conserved disulfide bond and being able to form the domain-swapped dimers. To identify structural features responsible for the formation of the bOBP unique dimeric structure and to understand the role of the domain swapping on maintaining the native structure of the protein, structural properties of the recombinant wild type bOBP and its mutant that cannot dimerize via the domain swapping were analyzed. We also looked at the effect of the disulfide bond by designing a monomeric bOBPs with restored disulfide bond which is conserved in other lipocalins. Finally, to understand which features in the microenvironment of the bOBP tryptophan residues play a role in the defining peculiarities of the intrinsic fluorescence of this protein we designed and investigated single-tryptophan mutants of the monomeric bOBP. Our analysis revealed that the insertion of the glycine after the residue 121 of the bOBP prevents domain swapping and generates a stable monomeric protein bOBP-Gly121+. We also show that the restored disulfide bond in the GCC-bOBP mutant leads to the noticeable stabilization of the monomeric structure. Structural and functional analysis revealed that none of the amino acid substitutions introduced to the bOBP affected functional activity of the protein and that the ligand binding leads to the formation of a more compact and stable state of the recombinant bOBP and its mutant monomeric forms. Finally, analysis of the single-tryptophan mutants of the monomeric bOBP gave us a unique possibility to find peculiarities of the microenvironment of tryptophan residues which were not previously described.

scholarly journals Structure and stability of recombinant bovine odorant-binding protein: I. Design and analysis of monomeric mutants

PeerJ ◽  
2016 ◽  
Vol 4 ◽  
pp. e1933 ◽  
Author(s):  
Olga V. Stepanenko ◽  
Denis O. Roginskii ◽  
Olesya V. Stepanenko ◽  
Irina M. Kuznetsova ◽  
Vladimir N. Uversky ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Binding Protein ◽  
Stable State ◽  
Structural Features ◽  
Odorant Binding Protein ◽  
Domain Swapping ◽  
Tryptophan Residues ◽  
Monomeric Structure ◽  
Odorant Binding

Bovine odorant-binding protein (bOBP) differs from other lipocalins by lacking the conserved disulfide bond and for being able to form the domain-swapped dimers. To identify structural features responsible for the formation of the bOBP unique dimeric structure and to understand the role of the domain swapping on maintaining the native structure of the protein, structural properties of the recombinant wild type bOBP and its mutant that cannot dimerize via the domain swapping were analyzed. We also looked at the effect of the disulfide bond by designing a monomeric bOBPs with restored disulfide bond which is conserved in other lipocalins. Finally, to understand which features in the microenvironment of the bOBP tryptophan residues play a role in the defining peculiarities of the intrinsic fluorescence of this protein we designed and investigated single-tryptophan mutants of the monomeric bOBP. Our analysis revealed that the insertion of the glycine after the residue 121 of the bOBP prevents domain swapping and generates a stable monomeric protein bOBP-Gly121+. We also show that the restored disulfide bond in the GCC-bOBP mutant leads to the noticeable stabilization of the monomeric structure. Structural and functional analysis revealed that none of the amino acid substitutions introduced to the bOBP affected functional activity of the protein and that the ligand binding leads to the formation of a more compact and stable state of the recombinant bOBP and its mutant monomeric forms. Finally, analysis of the single-tryptophan mutants of the monomeric bOBP gave us a unique possibility to find peculiarities of the microenvironment of tryptophan residues which were not previously described.

scholarly journals Structure and stability of recombinant bovine odorant-binding protein: I. Design and analysis of monomeric mutants

2015 ◽  
Author(s):  
Olga V Stepanenko ◽  
Denis O Roginskii ◽  
Olesya V Stepanenko ◽  
Irina M Kuznetsova ◽  
Vladimir N Uversky ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Binding Protein ◽  
Stable State ◽  
Structural Features ◽  
Odorant Binding Protein ◽  
Domain Swapping ◽  
Tryptophan Residues ◽  
Monomeric Structure ◽  
Odorant Binding

Bovine odorant-binding protein (bOBP) differs from other lipocalins by lacking the conserved disulfide bond and being able to form the domain-swapped dimers. To identify structural features responsible for the formation of the bOBP unique dimeric structure and to understand the role of the domain swapping on maintaining the native structure of the protein, structural properties of the recombinant wild type bOBP and its mutant that cannot dimerize via the domain swapping were analyzed. We also looked at the effect of the disulfide bond by designing a monomeric bOBPs with restored disulfide bond which is conserved in other lipocalins. Finally, to understand which features in the microenvironment of the bOBP tryptophan residues play a role in the defining peculiarities of the intrinsic fluorescence of this protein we designed and investigated single-tryptophan mutants of the monomeric bOBP. Our analysis revealed that the insertion of the glycine after the residue 121 of the bOBP prevents domain swapping and generates a stable monomeric protein bOBP-Gly121+. We also show that the restored disulfide bond in the GCC-bOBP mutant leads to the noticeable stabilization of the monomeric structure. Structural and functional analysis revealed that none of the amino acid substitutions introduced to the bOBP affected functional activity of the protein and that the ligand binding leads to the formation of a more compact and stable state of the recombinant bOBP and its mutant monomeric forms. Finally, analysis of the single-tryptophan mutants of the monomeric bOBP gave us a unique possibility to find peculiarities of the microenvironment of tryptophan residues which were not previously described.

scholarly journals Odorant-binding protein. Characterization of ligand binding.

1990 ◽  
Vol 265 (11) ◽  
pp. 6118-6125
Author(s):  
J Pevsner ◽  
V Hou ◽  
A M Snowman ◽  
S H Snyder
Keyword(s):  
Ligand Binding ◽  
Binding Protein ◽  
Protein Characterization ◽  
Odorant Binding Protein ◽  
Odorant Binding

Molecular and Functional Characterization of One Odorant-Binding Protein Gene OBP3 in Bemisia tabaci (Hemiptera: Aleyrodidae)

2019 ◽  
Author(s):  
Ran Wang ◽  
Yuan Hu ◽  
Peiling Wei ◽  
Cheng Qu ◽  
Chen Luo
Keyword(s):  
Host Plant ◽  
Bemisia Tabaci ◽  
Binding Protein ◽  
Insect Pest ◽  
Critical Role ◽  
Functional Characterization ◽  
Odorant Binding Protein ◽  
Binding Characteristics ◽  
And Function ◽  
Odorant Binding

Abstract Odorant binding proteins (OBPs) of insects play a critical role in chemical perceptions and choice of insect host plant. Bemisia tabaci is a notorious insect pest which can damage more than 600 plant species. In order to explore functions of OBPs in B. tabaci, here we investigated binding characteristics and function of odorant-binding protein 3 in B. tabaci (BtabOBP3). The results indicated that BtabOBP3 shows highly similar sequence with OBPs of other insects, including the typical signature motif of six cysteines. The recombinant BtabOBP3 protein was obtained, and the evaluation of binding affinities to tested volatiles of host plant was conducted, then the results indicated that β-ionone had significantly higher binding to BtabOBP3 among other tested plant volatiles. Furthermore, silencing of BtabOBP3 significantly altered choice behavior of B. tabaci to β-ionone. In conclusion, it has been demonstrated that BtabOBP3 exerts function as one carrier of β-ionone and the results could be contributed to reveal the mechanisms of choosing host plant in B. tabaci.

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