| 12 matches found in 4 documents. Search time: 0.883 seconds. |
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Score: 8.00 |
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| Title: Crystal structure of stable protein CutA1 from psychrotrophic bacterium Shewanella sp .
SIB1 .
| | Author: Sato A Yokotani S Tadokoro T Tanaka S Angkawidjaja C Koga Y Takano K Kanaya S | | Journal: J Synchrotron Radiat Citation: V : 18 P : 6-10 Year: 2011 Type: MEDLINE | | Literature: oryza Field: abstract Doc ID: pub21169681 Accession (PMID): 21169681 | | Abstract: CutA1 is widely found in bacteria , plants and animals , including humans .
The functions of CutA1 , however , have not been well clarified .
It is known that CutA1s from Pyrococcus horikoshii , Thermus thermophilus and Oryza sativa unfold at temperatures remarkably higher than the growth temperatures of the host organisms .
In this work the crystal structure of CutA1 from the psychrotrophic bacterium Shewanella sp .
SIB1 ( SIB1-CutA1 ) in a trimeric form was determined at 2 . 7 A resolution .
This is the first crystal structure of a psychrotrophic CutA1 .
The overall structure of SIB1-CutA1 is similar to those of CutA1 from Homo sapiens , Escherichia coli , Pyrococcus horikoshii , Thermus thermophilus , Termotoga maritima , Oryza sativa and Rattus norvergicus .
A peculiarity is observed in the beta2 strand .
The beta2 strand is divided into two short beta strands , beta2a and beta2b , in SIB1-CutA1 .
A thermal denaturation experiment revealed that SIB1-CutA1 does not unfold completely at 363 K at pH 7 . 0 , although Shewanella sp .
SIB1 can not grow at temperatures exceeding 303 K These results indicate that the trimeric structural motif of CutA1 is the critical factor in its unusually high stability and suggest that CutA1 needs to maintain its high stability in order to function , even in psychrotrophs .
| Matching Sentences:
[ Sen. 11, subscore: 2.00 ]: SIB1 can not grow at temperatures exceeding 303 K These results indicate that the trimeric structural motif of CutA1 is the critical factor in its unusually high stability and suggest that CutA1 needs to maintain its high stability in order to function , even in psychrotrophs .
[ Sen. 1, subscore: 1.00 ]: CutA1 is widely found in bacteria , plants and animals , including humans .
[ Sen. 2, subscore: 1.00 ]: The functions of CutA1 , however , have not been well clarified .
[ Sen. 3, subscore: 1.00 ]: It is known that CutA1s from Pyrococcus horikoshii , Thermus thermophilus and Oryza sativa unfold at temperatures remarkably higher than the growth temperatures of the host organisms .
[ Sen. 4, subscore: 1.00 ]: In this work the crystal structure of CutA1 from the psychrotrophic bacterium Shewanella sp .
[ Sen. 6, subscore: 1.00 ]: This is the first crystal structure of a psychrotrophic CutA1 .
[ Sen. 7, subscore: 1.00 ]: The overall structure of SIB1-CutA1 is similar to those of CutA1 from Homo sapiens , Escherichia coli , Pyrococcus horikoshii , Thermus thermophilus , Termotoga maritima , Oryza sativa and Rattus norvergicus .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 3.00 |
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| Title: Thermodynamic basis for the stabilities of three CutA1s from Pyrococcus horikoshii , Thermus thermophilus , and Oryza sativa , with unusually high denaturation temperatures .
| | Author: Sawano M Yamamoto H Ogasahara K Kidokoro S Katoh S Ohnuma T Katoh E Yokoyama S Yutani K | | Journal: Biochemistry Citation: V : 47 P : 721-30 Year: 2008 Type: MEDLINE | | Literature: oryza Field: abstract Doc ID: pub18154307 Accession (PMID): 18154307 | | Abstract: In order to elucidate the stabilization mechanism of CutA1 from Pyrococcus horikoshii ( PhCutA1 ) with a denaturation temperature of nearly 150 degrees C , GuHCl denaturation and heat denaturation were examined at neutral and acidic pHs .
As a comparison , CutA1 proteins from Thermus thermophilus ( TtCutA1 ) and Oryza sativa ( OsCutA1 ) were also examined , which have lower optimum growth temperatures of 75 and 28 degrees C , respectively , than that ( 98 degrees C ) of P horikoshii .
GuHCl-induced unfolding and refolding curves of the three proteins showed hysteresis effects due to an unusually slow unfolding rate .
The midpoints of refolding for PhCutA1 , TtCutA1 and OsCutA1 were 5 . 7 M , 3 . 3 M , and 2 . 3 M GuHCl , respectively , at pH 8 . 0 and 37 degrees C DSC experiments with TtCutA1 and OsCutA1 showed that the denaturation temperatures were remarkably high , 112 . 8 and 97 . 3 degrees C , respectively , at pH 7 . 0 and that the good heat reversibility was amenable to thermodynamic analyses .
At acidic pH , TtCutA1 showed higher stability to both heat and denaturant than PhCutA1 .
Combined with the data for DSC and denaturant denaturation , the unfolding Gibbs energy of PhCutA1 could be depicted as a function of temperature .
It was experimentally revealed that ( 1 ) the unusually high stability of PhCutA1 basically originates from a common trimer structure of the three proteins , ( 2 ) the stability of PhCutA1 is superior to those of the other two CutA1s over all temperatures above 0 degrees C at neutral pH , due to the decrease in both enthalpy and entropy , and ( 3 ) ion pairs of PhCutA1 contribute to the unusually high stability at neutral pH .
| Matching Sentences:
[ Sen. 1, subscore: 1.00 ]: In order to elucidate the stabilization mechanism of CutA1 from Pyrococcus horikoshii ( PhCutA1 ) with a denaturation temperature of nearly 150 degrees C , GuHCl denaturation and heat denaturation were examined at neutral and acidic pHs .
[ Sen. 2, subscore: 1.00 ]: As a comparison , CutA1 proteins from Thermus thermophilus ( TtCutA1 ) and Oryza sativa ( OsCutA1 ) were also examined , which have lower optimum growth temperatures of 75 and 28 degrees C , respectively , than that ( 98 degrees C ) of P horikoshii .
[ Sen. 7, subscore: 1.00 ]: It was experimentally revealed that ( 1 ) the unusually high stability of PhCutA1 basically originates from a common trimer structure of the three proteins , ( 2 ) the stability of PhCutA1 is superior to those of the other two CutA1s over all temperatures above 0 degrees C at neutral pH , due to the decrease in both enthalpy and entropy , and ( 3 ) ion pairs of PhCutA1 contribute to the unusually high stability at neutral pH .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 1.00 |
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| Title: Thermodynamic basis for the stabilities of three CutA1s from Pyrococcus horikoshii , Thermus thermophilus , and Oryza sativa , with unusually high denaturation temperatures .
| | Author: Sawano M Yamamoto H Ogasahara K Kidokoro S Katoh S Ohnuma T Katoh E Yokoyama S Yutani K | | Journal: Biochemistry Citation: V : 47 P : 721-30 Year: 2008 Type: MEDLINE | | Literature: oryza Field: title Doc ID: pub18154307 Accession (PMID): 18154307 | | Abstract: In order to elucidate the stabilization mechanism of CutA1 from Pyrococcus horikoshii ( PhCutA1 ) with a denaturation temperature of nearly 150 degrees C , GuHCl denaturation and heat denaturation were examined at neutral and acidic pHs .
As a comparison , CutA1 proteins from Thermus thermophilus ( TtCutA1 ) and Oryza sativa ( OsCutA1 ) were also examined , which have lower optimum growth temperatures of 75 and 28 degrees C , respectively , than that ( 98 degrees C ) of P horikoshii .
GuHCl-induced unfolding and refolding curves of the three proteins showed hysteresis effects due to an unusually slow unfolding rate .
The midpoints of refolding for PhCutA1 , TtCutA1 and OsCutA1 were 5 . 7 M , 3 . 3 M , and 2 . 3 M GuHCl , respectively , at pH 8 . 0 and 37 degrees C DSC experiments with TtCutA1 and OsCutA1 showed that the denaturation temperatures were remarkably high , 112 . 8 and 97 . 3 degrees C , respectively , at pH 7 . 0 and that the good heat reversibility was amenable to thermodynamic analyses .
At acidic pH , TtCutA1 showed higher stability to both heat and denaturant than PhCutA1 .
Combined with the data for DSC and denaturant denaturation , the unfolding Gibbs energy of PhCutA1 could be depicted as a function of temperature .
It was experimentally revealed that ( 1 ) the unusually high stability of PhCutA1 basically originates from a common trimer structure of the three proteins , ( 2 ) the stability of PhCutA1 is superior to those of the other two CutA1s over all temperatures above 0 degrees C at neutral pH , due to the decrease in both enthalpy and entropy , and ( 3 ) ion pairs of PhCutA1 contribute to the unusually high stability at neutral pH .
| Matching Sentences:
[ Sen. 1, subscore: 1.00 ]: Thermodynamic basis for the stabilities of three CutA1s from Pyrococcus horikoshii , Thermus thermophilus , and Oryza sativa , with unusually high denaturation temperatures .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
Score: 1.00 |
|---|
| Title: Crystal structure of stable protein CutA1 from psychrotrophic bacterium Shewanella sp .
SIB1 .
| | Author: Sato A Yokotani S Tadokoro T Tanaka S Angkawidjaja C Koga Y Takano K Kanaya S | | Journal: J Synchrotron Radiat Citation: V : 18 P : 6-10 Year: 2011 Type: MEDLINE | | Literature: oryza Field: title Doc ID: pub21169681 Accession (PMID): 21169681 | | Abstract: CutA1 is widely found in bacteria , plants and animals , including humans .
The functions of CutA1 , however , have not been well clarified .
It is known that CutA1s from Pyrococcus horikoshii , Thermus thermophilus and Oryza sativa unfold at temperatures remarkably higher than the growth temperatures of the host organisms .
In this work the crystal structure of CutA1 from the psychrotrophic bacterium Shewanella sp .
SIB1 ( SIB1-CutA1 ) in a trimeric form was determined at 2 . 7 A resolution .
This is the first crystal structure of a psychrotrophic CutA1 .
The overall structure of SIB1-CutA1 is similar to those of CutA1 from Homo sapiens , Escherichia coli , Pyrococcus horikoshii , Thermus thermophilus , Termotoga maritima , Oryza sativa and Rattus norvergicus .
A peculiarity is observed in the beta2 strand .
The beta2 strand is divided into two short beta strands , beta2a and beta2b , in SIB1-CutA1 .
A thermal denaturation experiment revealed that SIB1-CutA1 does not unfold completely at 363 K at pH 7 . 0 , although Shewanella sp .
SIB1 can not grow at temperatures exceeding 303 K These results indicate that the trimeric structural motif of CutA1 is the critical factor in its unusually high stability and suggest that CutA1 needs to maintain its high stability in order to function , even in psychrotrophs .
| Matching Sentences:
[ Sen. 1, subscore: 1.00 ]: Crystal structure of stable protein CutA1 from psychrotrophic bacterium Shewanella sp .
| | Supplemental links/files: reference in endnote online text related articles pubmed citation | |
