1idm

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(New page: 200px<br /><applet load="1idm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1idm, resolution 2.2&Aring;" /> '''3-ISOPROPYLMALATE DEH...)
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'''3-ISOPROPYLMALATE DEHYDROGENASE, LOOP-DELETED CHIMERA'''<br />
'''3-ISOPROPYLMALATE DEHYDROGENASE, LOOP-DELETED CHIMERA'''<br />
==Overview==
==Overview==
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A loop-deleted mutant form of 3-isopropylmalate dehydrogenase from Thermus, thermophilus was constructed to investigate the relationship between the, flexibility of the structure and the thermostability of the enzyme. The, structure of the mutant enzyme was determined by X-ray crystallography and, was found to be almost the same as that of the native enzyme with a, reduced temperature factor. Although the mutant protein had lost the, flexible loop, its function and thermostability had remained unchanged., This phenomenon can be explained by an internal reprieve tolerance, mechanism.
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A loop-deleted mutant form of 3-isopropylmalate dehydrogenase from Thermus thermophilus was constructed to investigate the relationship between the flexibility of the structure and the thermostability of the enzyme. The structure of the mutant enzyme was determined by X-ray crystallography and was found to be almost the same as that of the native enzyme with a reduced temperature factor. Although the mutant protein had lost the flexible loop, its function and thermostability had remained unchanged. This phenomenon can be explained by an internal reprieve tolerance mechanism.
==About this Structure==
==About this Structure==
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1IDM 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/3-isopropylmalate_dehydrogenase 3-isopropylmalate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.85 1.1.1.85] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IDM OCA].
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1IDM 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/3-isopropylmalate_dehydrogenase 3-isopropylmalate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.85 1.1.1.85] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IDM OCA].
==Reference==
==Reference==
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[[Category: chimera]]
[[Category: chimera]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:19:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:10:43 2008''

Revision as of 11:10, 21 February 2008


1idm, resolution 2.2Å

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3-ISOPROPYLMALATE DEHYDROGENASE, LOOP-DELETED CHIMERA

Overview

A loop-deleted mutant form of 3-isopropylmalate dehydrogenase from Thermus thermophilus was constructed to investigate the relationship between the flexibility of the structure and the thermostability of the enzyme. The structure of the mutant enzyme was determined by X-ray crystallography and was found to be almost the same as that of the native enzyme with a reduced temperature factor. Although the mutant protein had lost the flexible loop, its function and thermostability had remained unchanged. This phenomenon can be explained by an internal reprieve tolerance mechanism.

About this Structure

1IDM is a Single protein structure of sequence from Thermus thermophilus. Active as 3-isopropylmalate dehydrogenase, with EC number 1.1.1.85 Full crystallographic information is available from OCA.

Reference

Structure of a loop-deleted variant of 3-isopropylmalate dehydrogenase from Thermus thermophilus: an internal reprieve tolerance mechanism., Sakurai M, Ohzeki M, Miyazaki K, Moriyama H, Sato M, Tanaka N, Oshima T, Acta Crystallogr D Biol Crystallogr. 1996 Jan 1;52(Pt 1):124-8. PMID:15299733

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