1dr8
From Proteopedia
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- | [[Image:1dr8.jpg|left|200px]] | + | [[Image:1dr8.jpg|left|200px]] |
- | + | ||
- | '''STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD177''' | + | {{Structure |
+ | |PDB= 1dr8 |SIZE=350|CAPTION= <scene name='initialview01'>1dr8</scene>, resolution 2.70Å | ||
+ | |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= LEUB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | ||
+ | }} | ||
+ | |||
+ | '''STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD177''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1DR8 is a [ | + | 1DR8 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=1DR8 OCA]. |
==Reference== | ==Reference== | ||
- | Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships., Nurachman Z, Akanuma S, Sato T, Oshima T, Tanaka N, Protein Eng. 2000 Apr;13(4):253-8. PMID:[http:// | + | Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships., Nurachman Z, Akanuma S, Sato T, Oshima T, Tanaka N, Protein Eng. 2000 Apr;13(4):253-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10810156 10810156] |
[[Category: 3-isopropylmalate dehydrogenase]] | [[Category: 3-isopropylmalate dehydrogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: paperclip motion]] | [[Category: paperclip motion]] | ||
- | ''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 10:43:04 2008'' |
Revision as of 08:43, 20 March 2008
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, resolution 2.70Å | |||||||
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Gene: | LEUB (Thermus thermophilus) | ||||||
Activity: | 3-isopropylmalate dehydrogenase, with EC number 1.1.1.85 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD177
Overview
Thermal stability of the Thermus thermophilus isopropylmalate dehydrogenase enzyme was substantially lost upon the deletion of three residues from the C-terminus. However, the stability was partly recovered by the addition of two, four and seven amino acid residues (called HD177, HD708 and HD711, respectively) to the C-terminal region of the truncated enzyme. Three structures of these mutant enzymes were determined by an X-ray diffraction method. All protein crystals belong to space group P2(1) and their structures were solved by a standard molecular replacement method where the original dimer structure of the A172L mutant was used as a search model. Thermal stability of these mutant enzymes is discussed based on the 3D structure with special attention to the width of the active-site groove and the minor groove, distortion of beta-sheet pillar structure and size of cavity in the domain-domain interface around the C-terminus. Our previous studies revealed that the thermal stability of isopropylmalate dehydrogenase increases when the active-site cleft is closed (the closed form). In the present study it is shown that the active-site cleft can be regulated by open-close movement of the minor groove located at the opposite side to the active-site groove on the same subunit, through a paperclip-like motion.
About this Structure
1DR8 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Crystal structures of 3-isopropylmalate dehydrogenases with mutations at the C-terminus: crystallographic analyses of structure-stability relationships., Nurachman Z, Akanuma S, Sato T, Oshima T, Tanaka N, Protein Eng. 2000 Apr;13(4):253-8. PMID:10810156
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