Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae
TylP is one of five regulatory proteins involved in the regulation of antibiotic (tylosin) production, morphological and physiological differentiation in Streptomyces fradiae. Its function is similar to those of various γ-butyrolactone receptor proteins. In this report, N-terminally His-tagged recom...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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International Union of Crystallography
2017
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| Online Access: | http://psasir.upm.edu.my/id/eprint/59627/1/Crystallization%20and%20X-ray%20crystallographic%20analysis%20of%20recombinant%20TylP%2C%20a%20putative%20%CE%B3-butyrolactone%20receptor%20protein%20from%20Streptomyces%20fradiae.pdf |
| _version_ | 1825932037102501888 |
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| author | Mohd Sharif, Nurhikmah Shaibullah, Sofiyah Givajothi, Vasanthakumar Tan, Cheng Seng Ho, Kok Lian Teh, Aik Hong Baharum, Syarul Nataqain Waterman, Jitka Ng, Chyan Leong |
| author_facet | Mohd Sharif, Nurhikmah Shaibullah, Sofiyah Givajothi, Vasanthakumar Tan, Cheng Seng Ho, Kok Lian Teh, Aik Hong Baharum, Syarul Nataqain Waterman, Jitka Ng, Chyan Leong |
| author_sort | Mohd Sharif, Nurhikmah |
| collection | UPM |
| description | TylP is one of five regulatory proteins involved in the regulation of antibiotic (tylosin) production, morphological and physiological differentiation in Streptomyces fradiae. Its function is similar to those of various γ-butyrolactone receptor proteins. In this report, N-terminally His-tagged recombinant TylP protein (rTylP) was overproduced in Escherichia coli and purified to homogeneity. The rTylP protein was crystallized from a reservoir solution comprising 34%(v/v) ethylene glycol and 5%(v/v) glycerol. The protein crystals diffracted X-rays to 3.05 Å resolution and belonged to the trigonal space group P3121, with unit-cell parameters a = b = 126.62, c = 95.63 Å. |
| first_indexed | 2024-03-06T09:35:50Z |
| format | Article |
| id | upm.eprints-59627 |
| institution | Universiti Putra Malaysia |
| language | English |
| last_indexed | 2024-03-06T09:35:50Z |
| publishDate | 2017 |
| publisher | International Union of Crystallography |
| record_format | dspace |
| spelling | upm.eprints-596272018-03-14T03:01:43Z http://psasir.upm.edu.my/id/eprint/59627/ Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae Mohd Sharif, Nurhikmah Shaibullah, Sofiyah Givajothi, Vasanthakumar Tan, Cheng Seng Ho, Kok Lian Teh, Aik Hong Baharum, Syarul Nataqain Waterman, Jitka Ng, Chyan Leong TylP is one of five regulatory proteins involved in the regulation of antibiotic (tylosin) production, morphological and physiological differentiation in Streptomyces fradiae. Its function is similar to those of various γ-butyrolactone receptor proteins. In this report, N-terminally His-tagged recombinant TylP protein (rTylP) was overproduced in Escherichia coli and purified to homogeneity. The rTylP protein was crystallized from a reservoir solution comprising 34%(v/v) ethylene glycol and 5%(v/v) glycerol. The protein crystals diffracted X-rays to 3.05 Å resolution and belonged to the trigonal space group P3121, with unit-cell parameters a = b = 126.62, c = 95.63 Å. International Union of Crystallography 2017 Article PeerReviewed text en http://psasir.upm.edu.my/id/eprint/59627/1/Crystallization%20and%20X-ray%20crystallographic%20analysis%20of%20recombinant%20TylP%2C%20a%20putative%20%CE%B3-butyrolactone%20receptor%20protein%20from%20Streptomyces%20fradiae.pdf Mohd Sharif, Nurhikmah and Shaibullah, Sofiyah and Givajothi, Vasanthakumar and Tan, Cheng Seng and Ho, Kok Lian and Teh, Aik Hong and Baharum, Syarul Nataqain and Waterman, Jitka and Ng, Chyan Leong (2017) Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae. Acta Crystallographica Section F: Structural Biology Communications, 73 (2). pp. 109-115. ISSN 2053-230X http://onlinelibrary.wiley.com/doi/10.1107/S2053230X17001212/abstract 10.1107/S2053230X17001212 |
| spellingShingle | Mohd Sharif, Nurhikmah Shaibullah, Sofiyah Givajothi, Vasanthakumar Tan, Cheng Seng Ho, Kok Lian Teh, Aik Hong Baharum, Syarul Nataqain Waterman, Jitka Ng, Chyan Leong Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae |
| title | Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae |
| title_full | Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae |
| title_fullStr | Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae |
| title_full_unstemmed | Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae |
| title_short | Crystallization and X-ray crystallographic analysis of recombinant TylP, a putative γ-butyrolactone receptor protein from Streptomyces fradiae |
| title_sort | crystallization and x ray crystallographic analysis of recombinant tylp a putative γ butyrolactone receptor protein from streptomyces fradiae |
| url | http://psasir.upm.edu.my/id/eprint/59627/1/Crystallization%20and%20X-ray%20crystallographic%20analysis%20of%20recombinant%20TylP%2C%20a%20putative%20%CE%B3-butyrolactone%20receptor%20protein%20from%20Streptomyces%20fradiae.pdf |
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