1dr8

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[[Image:1dr8.jpg|left|200px]]<br /><applet load="1dr8" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1dr8.jpg|left|200px]]
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caption="1dr8, resolution 2.70&Aring;" />
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'''STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD177'''<br />
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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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|SITE=
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|LIGAND=
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|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]
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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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}}
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'''STRUCTURE OF MODIFIED 3-ISOPROPYLMALATE DEHYDROGENASE AT THE C-TERMINUS, HD177'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1DR8 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=1DR8 OCA].
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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==
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=10810156 10810156]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:38 2008''
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''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


PDB ID 1dr8

Drag the structure with the mouse to rotate
, resolution 2.70Å
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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