Entropic stabilization of the tryptophan synthase α-subunit from a hyperthermophile, Pyrococcus furiosus : X-ray analysis and calorimetry

Yamagata, Yuriko; Ogasahara, Kyoko; Hioki, Yusaku; Lee, Soo Jae; Nakagawa, Atushi; Nakamura, Haruyuki; Ishida, Masami; Kuramitsu, Seiki; Yutani, Katsuhide

doi:https://doi.org/10.1074/jbc.M009987200

Entropic stabilization of the tryptophan synthase α-subunit from a hyperthermophile, Pyrococcus furiosus : X-ray analysis and calorimetry

Yamagata, Yuriko; Ogasahara, Kyoko; Hioki, Yusaku et al.

Journal of Biological Chemistry, 2001, 276(14), 11062-11071

Number of Access:711（2025-09-29 10:04 Counts）

Identifier to cite or link to this item: https://hdl.handle.net/11094/73647

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Title	Entropic stabilization of the tryptophan synthase α-subunit from a hyperthermophile, Pyrococcus furiosus : X-ray analysis and calorimetry
Creator	NRID 1000040183678 1000040183678 CreatorName Yamagata, Yuriko
	CreatorName Ogasahara, Kyoko
	CreatorName Hioki, Yusaku
	CreatorName Lee, Soo Jae
	NRID 1000020188890 1000020188890 ORCID 0000-0002-1700-7861 0000-0002-1700-7861 researchmap permalink atsushi_nakagawa atsushi_nakagawa Scopus Author ID 7202934909 7202934909 CreatorName Nakagawa, Atushi
	CreatorName Nakamura, Haruyuki
	NRID 1000080223006 1000080223006 CreatorName Ishida, Masami
	NRID 1000060153368 1000060153368 CreatorName Kuramitsu, Seiki
	NRID 1000090089889 1000090089889 CreatorName Yutani, Katsuhide
Description	This research was originally published in Journal of Biological Chemistry. Yuriko Yamagata, Kyoko Ogasahara, Yusaku Hioki, Soo Jae Lee, Atsushi Nakagawa, Haruki Nakamura, Masami Ishida, Seiki Kuramitsui, and Katsuhide Yutani. Entropic stabilization of the tryptophan synthase α-subunit from a hyperthermophile, Pyrococcus furiosus : X-ray analysis and calorimetry. J. Biol. Chem. 2001; 276, 11062-11071. © the American Society for Biochemistry and Molecular Biology.
Abstract	The structure of the tryptophan synthase α-subunit from Pyrococcus furiosus was determined by x-ray analysis at 2.0-Å resolution, and its stability was examined by differential scanning calorimetry. Although the structure of the tryptophan synthase α_2β_2 complex from Salmonella typhimurium has been already determined, this is the first report of the structure of the α-subunit alone. The α-subunit from P. furiosus (Pf-α-subunit) lacked 12 and 6 residues at the N and C termini, respectively, and one residue each in two loop regions as compared with that from S. typhimurium (St-α-subunit), resulting in the absence of an N-terminal helix and the shortening of a C-terminal helix. The structure of the Pf-α-subunit was essentially similar to that of the St-asubunit in the α_2β_2 complex. The differences between both structures were discussed in connection with the higher stability of the Pf-α-subunit and the complex formation of the α- and β-subunits. Calorimetric results indicated that the Pf-α-subunit has extremely high thermostability and that its higher stability is caused by an entropic effect. On the basis of structural information of both proteins, we analyzed the contributions of each stabilization factor and could conclude that hydrophobic interactions in the protein interior do not contribute to the higher stability of the Pf-α-subunit. Rather, the increase in ion pairs, decrease in cavity volume, and entropic effects due to shortening of the polypeptide chain play important roles in extremely high stability in Pf-α-subunit.
Publisher	American Society for Biochemistry and Molecular Biology
Source Title	Journal of Biological Chemistry
Volume (Issue)	276(14)
Page	11062-11071
Date of Issued	2001-04
Language	English
Handle URL	https://hdl.handle.net/11094/73647
eISSN	1083351X
NCID	AA1202441X
Relation.isIdenticalTo	DOI (Publisher Version) https://doi.org/10.1074/jbc.M009987200
Relation.isIdenticalTo	PMID 11118452
Access Rights	open access
CopyRight	© the American Society for Biochemistry and Molecular Biology.
oaire:version	Version of Record
Category	学術雑誌論文 Journal Article

Resource Type	journal article
Local Type	Journal Article
DCMI Type	Text
DCTERMS.bibliographicCitation	Journal of Biological Chemistry. 2001, 276(14), p. 11062-11071
DC.title	Entropic stabilization of the tryptophan synthase α-subunit from a hyperthermophile, Pyrococcus furiosus : X-ray analysis and calorimetry
DC.creator	Yamagata, Yuriko
	Ogasahara, Kyoko
	Hioki, Yusaku
	Lee, Soo Jae
	Nakagawa, Atushi
	Nakamura, Haruyuki
	Ishida, Masami
	Kuramitsu, Seiki
	Yutani, Katsuhide
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	English
DC.type' scheme='DCTERMS.DCMIType	Text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2001-04
DC.identifier	https://doi.org/10.1074/jbc.M009987200
DC.description	This research was originally published in Journal of Biological Chemistry. Yuriko Yamagata, Kyoko Ogasahara, Yusaku Hioki, Soo Jae Lee, Atsushi Nakagawa, Haruki Nakamura, Masami Ishida, Seiki Kuramitsui, and Katsuhide Yutani. Entropic stabilization of the tryptophan synthase α-subunit from a hyperthermophile, Pyrococcus furiosus : X-ray analysis and calorimetry. J. Biol. Chem. 2001; 276, 11062-11071. © the American Society for Biochemistry and Molecular Biology.
DCTERMS.abstract	The structure of the tryptophan synthase α-subunit from Pyrococcus furiosus was determined by x-ray analysis at 2.0-Å resolution, and its stability was examined by differential scanning calorimetry. Although the structure of the tryptophan synthase α_2β_2 complex from Salmonella typhimurium has been already determined, this is the first report of the structure of the α-subunit alone. The α-subunit from P. furiosus (Pf-α-subunit) lacked 12 and 6 residues at the N and C termini, respectively, and one residue each in two loop regions as compared with that from S. typhimurium (St-α-subunit), resulting in the absence of an N-terminal helix and the shortening of a C-terminal helix. The structure of the Pf-α-subunit was essentially similar to that of the St-asubunit in the α_2β_2 complex. The differences between both structures were discussed in connection with the higher stability of the Pf-α-subunit and the complex formation of the α- and β-subunits. Calorimetric results indicated that the Pf-α-subunit has extremely high thermostability and that its higher stability is caused by an entropic effect. On the basis of structural information of both proteins, we analyzed the contributions of each stabilization factor and could conclude that hydrophobic interactions in the protein interior do not contribute to the higher stability of the Pf-α-subunit. Rather, the increase in ion pairs, decrease in cavity volume, and entropic effects due to shortening of the polypeptide chain play important roles in extremely high stability in Pf-α-subunit.
DC.rights	© the American Society for Biochemistry and Molecular Biology.
DC.format	73647
citation_title	Entropic stabilization of the tryptophan synthase α-subunit from a hyperthermophile, Pyrococcus furiosus : X-ray analysis and calorimetry
citation_author	Yamagata, Yuriko
	Ogasahara, Kyoko
	Hioki, Yusaku
	Lee, Soo Jae
	Nakagawa, Atushi
	Nakamura, Haruyuki
	Ishida, Masami
	Kuramitsu, Seiki
	Yutani, Katsuhide
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	English
citation_date	2001-04
citation_journal_title	Journal of Biological Chemistry
citation_volume	276
citation_issue	14
citation_firstpage	11062
citation_lastpage	11071
citation_doi	https://doi.org/10.1074/jbc.M009987200
citation_pmid	11118452
citation_public_url	https://hdl.handle.net/11094/73647

Entropic stabilization of the tryptophan synthase α-subunit from a hyperthermophile, Pyrococcus furiosus : X-ray analysis and calorimetry

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