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| | {{STRUCTURE_1geq| PDB=1geq | SCENE= }} | | {{STRUCTURE_1geq| PDB=1geq | SCENE= }} |
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| - | '''Entropic stabilization of the tryptophan synthase A-subunit from a hyperthermophile, pyrococcus furiosus: X-ray analysis and calorimetry'''
| + | ===Entropic stabilization of the tryptophan synthase A-subunit from a hyperthermophile, pyrococcus furiosus: X-ray analysis and calorimetry=== |
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| - | ==Overview==
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| - | The structure of the tryptophan synthase alpha-subunit from Pyrococcus furiosus was determined by x-ray analysis at 2.0-A resolution, and its stability was examined by differential scanning calorimetry. Although the structure of the tryptophan synthase alpha(2)beta(2) complex from Salmonella typhimurium has been already determined, this is the first report of the structure of the alpha-subunit alone. The alpha-subunit from P. furiosus (Pf-alpha-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-alpha-subunit), resulting in the absence of an N-terminal helix and the shortening of a C-terminal helix. The structure of the Pf-alpha-subunit was essentially similar to that of the St-alpha-subunit in the alpha(2)beta(2) complex. The differences between both structures were discussed in connection with the higher stability of the Pf-alpha-subunit and the complex formation of the alpha- and beta-subunits. Calorimetric results indicated that the Pf-alpha-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-alpha-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-alpha-subunit. | + | The line below this paragraph, {{ABSTRACT_PUBMED_11118452}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11118452 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11118452}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Tryptophan synthase alpha-subunit]] | | [[Category: Tryptophan synthase alpha-subunit]] |
| | [[Category: X-ray analysis]] | | [[Category: X-ray analysis]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 7 08:40:07 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:10:48 2008'' |
Revision as of 02:10, 1 July 2008
Template:STRUCTURE 1geq
Entropic stabilization of the tryptophan synthase A-subunit from a hyperthermophile, pyrococcus furiosus: X-ray analysis and calorimetry
Template:ABSTRACT PUBMED 11118452
About this Structure
1GEQ is a Single protein structure of sequence from Pyrococcus furiosus. Full crystallographic information is available from OCA.
Reference
Entropic stabilization of the tryptophan synthase alpha-subunit from a hyperthermophile, Pyrococcus furiosus. X-ray analysis and calorimetry., Yamagata Y, Ogasahara K, Hioki Y, Lee SJ, Nakagawa A, Nakamura H, Ishida M, Kuramitsu S, Yutani K, J Biol Chem. 2001 Apr 6;276(14):11062-71. Epub 2000 Dec 15. PMID:11118452
Page seeded by OCA on Tue Jul 1 05:10:48 2008
