1jl1
From Proteopedia
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| - | [[Image:1jl1.jpg|left|200px]] | + | [[Image:1jl1.jpg|left|200px]] |
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| - | '''D10A E. coli ribonuclease HI''' | + | {{Structure |
| + | |PDB= 1jl1 |SIZE=350|CAPTION= <scene name='initialview01'>1jl1</scene>, resolution 1.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''D10A E. coli ribonuclease HI''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JL1 is a [ | + | 1JL1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JL1 OCA]. |
==Reference== | ==Reference== | ||
| - | Native-state energetics of a thermostabilized variant of ribonuclease HI., Goedken ER, Marqusee S, J Mol Biol. 2001 Dec 7;314(4):863-71. PMID:[http:// | + | Native-state energetics of a thermostabilized variant of ribonuclease HI., Goedken ER, Marqusee S, J Mol Biol. 2001 Dec 7;314(4):863-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11734003 11734003] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Ribonuclease H]] | [[Category: Ribonuclease H]] | ||
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[[Category: thermostability]] | [[Category: thermostability]] | ||
| - | ''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 12:04:50 2008'' |
Revision as of 10:04, 20 March 2008
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| , resolution 1.3Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Ribonuclease H, with EC number 3.1.26.4 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
D10A E. coli ribonuclease HI
Overview
Escherichia coli RNase HI is a well-characterized model system for protein folding and stability. Controlling protein stability is critical for both natural proteins and for the development of engineered proteins that function under extreme conditions. We have used native-state hydrogen exchange on a variant containing the stabilizing mutation Asp10 to alanine in order to determine its residue-specific stabilities. On average, the DeltaG(unf) value for each residue was increased by 2-3 kcal/mol, resulting in a lower relative population of partially unfolded forms. Though increased in stability by a uniform factor, D10A shows a distribution of stabilities in its secondary structural units that is similar to that of E. coli RNase H, but not the closely related protein from Thermus thermophilus. Hence, the simple mutation used to stabilize the enzyme does not recreate the balance of conformational flexibility evolved in the thermophilic protein.
About this Structure
1JL1 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Native-state energetics of a thermostabilized variant of ribonuclease HI., Goedken ER, Marqusee S, J Mol Biol. 2001 Dec 7;314(4):863-71. PMID:11734003
Page seeded by OCA on Thu Mar 20 12:04:50 2008
