1v5x

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(New page: 200px<br /><applet load="1v5x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v5x, resolution 2.00&Aring;" /> '''Crystal structure of...)
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[[Image:1v5x.jpg|left|200px]]<br /><applet load="1v5x" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1v5x, resolution 2.00&Aring;" />
caption="1v5x, resolution 2.00&Aring;" />
'''Crystal structure of Phosphoribosyl anthranilate isomerase from Thermus Thermophilus'''<br />
'''Crystal structure of Phosphoribosyl anthranilate isomerase from Thermus Thermophilus'''<br />
==Overview==
==Overview==
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The crystal structure of phosphoribosyl anthranilate isomerase (PRAI) from, Thermus thermophilus HB8 (TtPRAI) was solved at 2.0 A resolution. The, overall structure of TtPRAI with a dimeric structure was quite similar to, that of PRAI from Thermotoga maritima (TmPRAI). In order to elucidate the, stabilization mechanism of TtPRAI, its physicochemical properties were, examined using DSC, CD, and analytical centrifugation at various pHs in, relation to the association-dissociation of the subunits. Based on the, experimental results for TtPRAI and the structural information on TtPRAI, and TmPRAI, we found that: (i) the denaturation of TtPRAI at acidic pH is, correlated with the dissociation of its dimeric form; (ii) the hydrophobic, interaction of TtPRAI in the monomer structure is slightly greater than, that of TmPRAI, but dimer interface of the TmPRAI is remarkably greater;, (iii) the contributions of hydrogen bonds and ion bonds to the stability, are similar to each other; and (iv) destabilization due to the presence of, cavities in TtPRAI is greater than that of TmPRAI in both the monomer and, dimer structures.
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The crystal structure of phosphoribosyl anthranilate isomerase (PRAI) from Thermus thermophilus HB8 (TtPRAI) was solved at 2.0 A resolution. The overall structure of TtPRAI with a dimeric structure was quite similar to that of PRAI from Thermotoga maritima (TmPRAI). In order to elucidate the stabilization mechanism of TtPRAI, its physicochemical properties were examined using DSC, CD, and analytical centrifugation at various pHs in relation to the association-dissociation of the subunits. Based on the experimental results for TtPRAI and the structural information on TtPRAI and TmPRAI, we found that: (i) the denaturation of TtPRAI at acidic pH is correlated with the dissociation of its dimeric form; (ii) the hydrophobic interaction of TtPRAI in the monomer structure is slightly greater than that of TmPRAI, but dimer interface of the TmPRAI is remarkably greater; (iii) the contributions of hydrogen bonds and ion bonds to the stability are similar to each other; and (iv) destabilization due to the presence of cavities in TtPRAI is greater than that of TmPRAI in both the monomer and dimer structures.
==About this Structure==
==About this Structure==
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1V5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/Phosphoribosylanthranilate_isomerase Phosphoribosylanthranilate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.24 5.3.1.24] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V5X OCA].
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1V5X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/Phosphoribosylanthranilate_isomerase Phosphoribosylanthranilate isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.1.24 5.3.1.24] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1V5X OCA].
==Reference==
==Reference==
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Stabilization due to dimer formation of phosphoribosyl anthranilate isomerase from Thermus thermophilus HB8: X-ray Analysis and DSC experiments., Taka J, Ogasahara K, Jeyakanthan J, Kunishima N, Kuroishi C, Sugahara M, Yokoyama S, Yutani K, J Biochem (Tokyo). 2005 May;137(5):569-78. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15944409 15944409]
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Stabilization due to dimer formation of phosphoribosyl anthranilate isomerase from Thermus thermophilus HB8: X-ray Analysis and DSC experiments., Taka J, Ogasahara K, Jeyakanthan J, Kunishima N, Kuroishi C, Sugahara M, Yokoyama S, Yutani K, J Biochem. 2005 May;137(5):569-78. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15944409 15944409]
[[Category: Phosphoribosylanthranilate isomerase]]
[[Category: Phosphoribosylanthranilate isomerase]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[Category: Kunishima, N.]]
[[Category: Kunishima, N.]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Taka, J.]]
[[Category: Taka, J.]]
[[Category: Yutani, K.]]
[[Category: Yutani, K.]]
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[[Category: trpf]]
[[Category: trpf]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:37:51 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:31:49 2008''

Revision as of 13:31, 21 February 2008


1v5x, resolution 2.00Å

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Crystal structure of Phosphoribosyl anthranilate isomerase from Thermus Thermophilus

Overview

The crystal structure of phosphoribosyl anthranilate isomerase (PRAI) from Thermus thermophilus HB8 (TtPRAI) was solved at 2.0 A resolution. The overall structure of TtPRAI with a dimeric structure was quite similar to that of PRAI from Thermotoga maritima (TmPRAI). In order to elucidate the stabilization mechanism of TtPRAI, its physicochemical properties were examined using DSC, CD, and analytical centrifugation at various pHs in relation to the association-dissociation of the subunits. Based on the experimental results for TtPRAI and the structural information on TtPRAI and TmPRAI, we found that: (i) the denaturation of TtPRAI at acidic pH is correlated with the dissociation of its dimeric form; (ii) the hydrophobic interaction of TtPRAI in the monomer structure is slightly greater than that of TmPRAI, but dimer interface of the TmPRAI is remarkably greater; (iii) the contributions of hydrogen bonds and ion bonds to the stability are similar to each other; and (iv) destabilization due to the presence of cavities in TtPRAI is greater than that of TmPRAI in both the monomer and dimer structures.

About this Structure

1V5X is a Single protein structure of sequence from Thermus thermophilus. Active as Phosphoribosylanthranilate isomerase, with EC number 5.3.1.24 Full crystallographic information is available from OCA.

Reference

Stabilization due to dimer formation of phosphoribosyl anthranilate isomerase from Thermus thermophilus HB8: X-ray Analysis and DSC experiments., Taka J, Ogasahara K, Jeyakanthan J, Kunishima N, Kuroishi C, Sugahara M, Yokoyama S, Yutani K, J Biochem. 2005 May;137(5):569-78. PMID:15944409

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