1ujp
From Proteopedia
(New page: 200px<br /><applet load="1ujp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ujp, resolution 1.34Å" /> '''Crystal Structure of...) |
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| - | [[Image:1ujp.jpg|left|200px]]<br /><applet load="1ujp" size=" | + | [[Image:1ujp.jpg|left|200px]]<br /><applet load="1ujp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ujp, resolution 1.34Å" /> | caption="1ujp, resolution 1.34Å" /> | ||
'''Crystal Structure of Tryptophan Synthase A-Subunit From Thermus thermophilus HB8'''<br /> | '''Crystal Structure of Tryptophan Synthase A-Subunit From Thermus thermophilus HB8'''<br /> | ||
==Overview== | ==Overview== | ||
| - | In order to elucidate the thermo-stabilization mechanism of the tryptophan | + | In order to elucidate the thermo-stabilization mechanism of the tryptophan synthase alpha-subunit from the extreme thermophile Thermus thermophilus HB8 (Tt-alpha-subunit), its crystal structure was determined and its stability was examined using DSC. The results were compared to those of other orthologs from mesophilic and hyperthermophilic organisms. The denaturation temperature of the Tt-alpha-subunit was higher than that of the alpha-subunit from S. typhimurium (St-alpha-subunit) but lower than that of the alpha-subunit from P. furiosus (Pf-alpha-subunit). Specific denaturation enthalpy and specific denaturation heat capacity values of the Tt-alpha-subunit were the lowest among the three proteins, suggesting that entropy effects are responsible for the stabilization of the Tt-alpha-subunit. Based on a structural comparison with the St-alpha-subunit, two deletions in loop regions, an increase in the number of ion pairs and a decrease in cavity volume seem to be responsible for the stabilization of the Tt-alpha-subunit. The results of structural comparison suggest that the native structure of the Tt-alpha-subunit is better adapted to an ideally stable structure than that of the St-alpha-subunit, but worse than that of the Pf-alpha-subunit. The results of calorimetry suggest that the residual structure of the Tt-alpha-subunit in the denatured state contributes to the stabilization. |
==About this Structure== | ==About this Structure== | ||
| - | 1UJP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with CIT as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] Full crystallographic information is available from [http:// | + | 1UJP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus] with <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Tryptophan_synthase Tryptophan synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.20 4.2.1.20] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UJP OCA]. |
==Reference== | ==Reference== | ||
| - | Stabilization mechanism of the tryptophan synthase alpha-subunit from Thermus thermophilus HB8: X-ray crystallographic analysis and calorimetry., Asada Y, Sawano M, Ogasahara K, Nakamura J, Ota M, Kuroishi C, Sugahara M, Yutani K, Kunishima N, J Biochem | + | Stabilization mechanism of the tryptophan synthase alpha-subunit from Thermus thermophilus HB8: X-ray crystallographic analysis and calorimetry., Asada Y, Sawano M, Ogasahara K, Nakamura J, Ota M, Kuroishi C, Sugahara M, Yutani K, Kunishima N, J Biochem. 2005 Oct;138(4):343-53. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16272128 16272128] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
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[[Category: Kuramitsu, S.]] | [[Category: Kuramitsu, S.]] | ||
[[Category: Miyano, M.]] | [[Category: Miyano, M.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
[[Category: CIT]] | [[Category: CIT]] | ||
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[[Category: tryptophan synthase]] | [[Category: tryptophan synthase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:25:12 2008'' |
Revision as of 13:25, 21 February 2008
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Crystal Structure of Tryptophan Synthase A-Subunit From Thermus thermophilus HB8
Overview
In order to elucidate the thermo-stabilization mechanism of the tryptophan synthase alpha-subunit from the extreme thermophile Thermus thermophilus HB8 (Tt-alpha-subunit), its crystal structure was determined and its stability was examined using DSC. The results were compared to those of other orthologs from mesophilic and hyperthermophilic organisms. The denaturation temperature of the Tt-alpha-subunit was higher than that of the alpha-subunit from S. typhimurium (St-alpha-subunit) but lower than that of the alpha-subunit from P. furiosus (Pf-alpha-subunit). Specific denaturation enthalpy and specific denaturation heat capacity values of the Tt-alpha-subunit were the lowest among the three proteins, suggesting that entropy effects are responsible for the stabilization of the Tt-alpha-subunit. Based on a structural comparison with the St-alpha-subunit, two deletions in loop regions, an increase in the number of ion pairs and a decrease in cavity volume seem to be responsible for the stabilization of the Tt-alpha-subunit. The results of structural comparison suggest that the native structure of the Tt-alpha-subunit is better adapted to an ideally stable structure than that of the St-alpha-subunit, but worse than that of the Pf-alpha-subunit. The results of calorimetry suggest that the residual structure of the Tt-alpha-subunit in the denatured state contributes to the stabilization.
About this Structure
1UJP is a Single protein structure of sequence from Thermus thermophilus with as ligand. Active as Tryptophan synthase, with EC number 4.2.1.20 Full crystallographic information is available from OCA.
Reference
Stabilization mechanism of the tryptophan synthase alpha-subunit from Thermus thermophilus HB8: X-ray crystallographic analysis and calorimetry., Asada Y, Sawano M, Ogasahara K, Nakamura J, Ota M, Kuroishi C, Sugahara M, Yutani K, Kunishima N, J Biochem. 2005 Oct;138(4):343-53. PMID:16272128
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