Crystal structures of Val58Ile tryptophan repressor in a domain-swapped array in the presence and absence of l-tryptophan Sprenger Janina
(2021) In Acta Crystallographica Section F: Structural Biology Communications 77. p.215-225- Abstract
The crystal structures of domain-swapped tryptophan repressor (TrpR) variant Val58Ile before and after soaking with the physiological ligand l-tryptophan (l-Trp) indicate that l-Trp occupies the same location in the domain-swapped form as in native dimeric TrpR and makes equivalent residue contacts. This result is unexpected because the ligand binding-site residues arise from three separate polypeptide chains in the domain-swapped form. This work represents the first published structure of a domain-swapped form of TrpR with l-Trp bound. The presented structures also show that the protein amino-terminus, whether or not it bears a disordered extension of about 20 residues, is accessible in the large solvent channels of the domain-swapped... (More)
The crystal structures of domain-swapped tryptophan repressor (TrpR) variant Val58Ile before and after soaking with the physiological ligand l-tryptophan (l-Trp) indicate that l-Trp occupies the same location in the domain-swapped form as in native dimeric TrpR and makes equivalent residue contacts. This result is unexpected because the ligand binding-site residues arise from three separate polypeptide chains in the domain-swapped form. This work represents the first published structure of a domain-swapped form of TrpR with l-Trp bound. The presented structures also show that the protein amino-terminus, whether or not it bears a disordered extension of about 20 residues, is accessible in the large solvent channels of the domain-swapped crystal form, as in the structures reported previously in this form for TrpR without N-terminal extensions. These findings inspire the exploration of l-Trp analogs and N-terminal modifications as labels to orient guest proteins that cannot otherwise be crystallized in the solvent channels of crystalline domain-swapped TrpR hosts for potential diffraction analysis.
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- author
- Sprenger, Janina LU ; Lawson, Catherine L. ; Von Wachenfeldt, Claes LU ; Leggio, Leila Lo and Carey, Jannette LU
- organization
- publishing date
- 2021
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- crystalline protein gel, domain swapping, fragment-based screening, hostal system, ligand binding, molecular baits, Val58Ile tryptophan repressor
- in
- Acta Crystallographica Section F: Structural Biology Communications
- volume
- 77
- pages
- 11 pages
- publisher
- Wiley-Blackwell
- external identifiers
-
- scopus:85109187829
- pmid:34196612
- ISSN
- 2053-230X
- DOI
- 10.1107/S2053230X21006142
- language
- English
- LU publication?
- yes
- id
- 9fd61391-7749-459e-b5a4-741140d9b4d0
- date added to LUP
- 2021-08-18 16:21:33
- date last changed
- 2024-03-23 08:04:36
@article{9fd61391-7749-459e-b5a4-741140d9b4d0,
abstract = {{<p>The crystal structures of domain-swapped tryptophan repressor (TrpR) variant Val58Ile before and after soaking with the physiological ligand l-tryptophan (l-Trp) indicate that l-Trp occupies the same location in the domain-swapped form as in native dimeric TrpR and makes equivalent residue contacts. This result is unexpected because the ligand binding-site residues arise from three separate polypeptide chains in the domain-swapped form. This work represents the first published structure of a domain-swapped form of TrpR with l-Trp bound. The presented structures also show that the protein amino-terminus, whether or not it bears a disordered extension of about 20 residues, is accessible in the large solvent channels of the domain-swapped crystal form, as in the structures reported previously in this form for TrpR without N-terminal extensions. These findings inspire the exploration of l-Trp analogs and N-terminal modifications as labels to orient guest proteins that cannot otherwise be crystallized in the solvent channels of crystalline domain-swapped TrpR hosts for potential diffraction analysis. </p>}},
author = {{Sprenger, Janina and Lawson, Catherine L. and Von Wachenfeldt, Claes and Leggio, Leila Lo and Carey, Jannette}},
issn = {{2053-230X}},
keywords = {{crystalline protein gel; domain swapping; fragment-based screening; hostal system; ligand binding; molecular baits; Val58Ile tryptophan repressor}},
language = {{eng}},
pages = {{215--225}},
publisher = {{Wiley-Blackwell}},
series = {{Acta Crystallographica Section F: Structural Biology Communications}},
title = {{Crystal structures of Val58Ile tryptophan repressor in a domain-swapped array in the presence and absence of l-tryptophan Sprenger Janina}},
url = {{http://dx.doi.org/10.1107/S2053230X21006142}},
doi = {{10.1107/S2053230X21006142}},
volume = {{77}},
year = {{2021}},
}