1dr8

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[[Image:1dr8.jpg|left|200px]]
[[Image:1dr8.jpg|left|200px]]
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{{Structure
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|PDB= 1dr8 |SIZE=350|CAPTION= <scene name='initialview01'>1dr8</scene>, resolution 2.70&Aring;
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The line below this paragraph, containing "STRUCTURE_1dr8", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND=
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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|GENE= LEUB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus])
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|DOMAIN=
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{{STRUCTURE_1dr8| PDB=1dr8 | SCENE= }}
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|RELATEDENTRY=[[1osj|1OSJ]], [[1dpz|1DPZ]], [[1dr0|1DR0]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dr8 OCA], [http://www.ebi.ac.uk/pdbsum/1dr8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1dr8 RCSB]</span>
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'''STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD177'''
'''STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD177'''
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[[Category: Sato, T.]]
[[Category: Sato, T.]]
[[Category: Tanaka, N.]]
[[Category: Tanaka, N.]]
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[[Category: dehydrogenase]]
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[[Category: Dehydrogenase]]
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[[Category: minor groove]]
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[[Category: Minor groove]]
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[[Category: paperclip motion]]
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[[Category: Paperclip motion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:11:04 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:47:09 2008''
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Revision as of 11:11, 2 May 2008

Template:STRUCTURE 1dr8

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 Page seeded by OCA on Fri May 2 14:11:04 2008

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