1xac
From Proteopedia
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| - | [[Image:1xac.gif|left|200px]] | + | [[Image:1xac.gif|left|200px]] |
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| - | '''CHIMERA ISOPROPYLMALATE DEHYDROGENASE BETWEEN BACILLUS SUBTILIS (M) AND THERMUS THERMOPHILUS (T) FROM N-TERMINAL: 20% T MIDDLE 20% M RESIDUAL 60% T, MUTATED AT S82R. LOW TEMPERATURE (100K) STRUCTURE.''' | + | {{Structure |
| + | |PDB= 1xac |SIZE=350|CAPTION= <scene name='initialview01'>1xac</scene>, resolution 2.1Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CHIMERA ISOPROPYLMALATE DEHYDROGENASE BETWEEN BACILLUS SUBTILIS (M) AND THERMUS THERMOPHILUS (T) FROM N-TERMINAL: 20% T MIDDLE 20% M RESIDUAL 60% T, MUTATED AT S82R. LOW TEMPERATURE (100K) STRUCTURE.''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1XAC is a [ | + | 1XAC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XAC OCA]. |
==Reference== | ==Reference== | ||
| - | Cryocrystallography of 3-Isopropylmalate dehydrogenase from Thermus thermophilus and its chimeric enzyme., Nagata C, Moriyama H, Tanaka N, Nakasako M, Yamamoto M, Ueki T, Oshima T, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):623-30. PMID:[http:// | + | Cryocrystallography of 3-Isopropylmalate dehydrogenase from Thermus thermophilus and its chimeric enzyme., Nagata C, Moriyama H, Tanaka N, Nakasako M, Yamamoto M, Ueki T, Oshima T, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):623-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15299625 15299625] |
[[Category: 3-isopropylmalate dehydrogenase]] | [[Category: 3-isopropylmalate dehydrogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:07:08 2008'' |
Revision as of 13:07, 20 March 2008
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| , resolution 2.1Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | 3-isopropylmalate dehydrogenase, with EC number 1.1.1.85 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CHIMERA ISOPROPYLMALATE DEHYDROGENASE BETWEEN BACILLUS SUBTILIS (M) AND THERMUS THERMOPHILUS (T) FROM N-TERMINAL: 20% T MIDDLE 20% M RESIDUAL 60% T, MUTATED AT S82R. LOW TEMPERATURE (100K) STRUCTURE.
Overview
The crystal structures of thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus (10T) and a chimeric enzyme between T. thermophilus and Bacillus subtilus with one point mutation (cS82R), were determined at both 100 and 150 K. At the cryogenic condition, the volume of the unit cell decreased by 5% as a result of a contraction in the solvent region. Although the overall structures of both enzymes at low temperature were the same as that of 10T at room temperature, interactions between two domains and between two subunits in a functional dimer of cS82R were significantly altered. The decrease in the average temperature factor of 10T at low temperature and no significant decrease for cS82R suggested that the structure of the engineered enzyme (cS82R) may have many conformational substates even at low temperature, while the native enzyme (10T) at low temperature has a more definite conformation than that at room temperature. The location of water molecules around the enzyme molecule and the calculation of the radii of gyration suggested that cS82R had a weaker hydration than 10T.
About this Structure
1XAC is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Cryocrystallography of 3-Isopropylmalate dehydrogenase from Thermus thermophilus and its chimeric enzyme., Nagata C, Moriyama H, Tanaka N, Nakasako M, Yamamoto M, Ueki T, Oshima T, Acta Crystallogr D Biol Crystallogr. 1996 Jul 1;52(Pt 4):623-30. PMID:15299625
Page seeded by OCA on Thu Mar 20 15:07:08 2008
