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1rkn
From Proteopedia
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| - | [[Image:1rkn.gif|left|200px]] | + | [[Image:1rkn.gif|left|200px]] |
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| - | '''Solution structure of 1-110 fragment of Staphylococcal Nuclease with G88W mutation''' | + | {{Structure |
| + | |PDB= 1rkn |SIZE=350|CAPTION= <scene name='initialview01'>1rkn</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Micrococcal_nuclease Micrococcal nuclease], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.31.1 3.1.31.1] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Solution structure of 1-110 fragment of Staphylococcal Nuclease with G88W mutation''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RKN is a [ | + | 1RKN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RKN OCA]. |
==Reference== | ==Reference== | ||
| - | Folding stability and cooperativity of the three forms of 1-110 residues fragment of staphylococcal nuclease., Xie T, Liu D, Feng Y, Shan L, Wang J, Biophys J. 2007 Mar 15;92(6):2090-107. Epub 2006 Dec 15. PMID:[http:// | + | Folding stability and cooperativity of the three forms of 1-110 residues fragment of staphylococcal nuclease., Xie T, Liu D, Feng Y, Shan L, Wang J, Biophys J. 2007 Mar 15;92(6):2090-107. Epub 2006 Dec 15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17172296 17172296] |
[[Category: Micrococcal nuclease]] | [[Category: Micrococcal nuclease]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: staphylococcal nuclease]] | [[Category: staphylococcal nuclease]] | ||
| - | ''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 13:52:56 2008'' |
Revision as of 11:52, 20 March 2008
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| Activity: | Micrococcal nuclease, with EC number 3.1.31.1 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of 1-110 fragment of Staphylococcal Nuclease with G88W mutation
Overview
Folding stability and cooperativity of the three forms of 1-110 residues fragment of staphylococcal nuclease (SNase110) have been studied by various biophysical and NMR methods. Samples of G-88W- and V-66W-mutant SNase110, namely G-88W110 and V-66W110, in aqueous solution and SNase110 in 2.0 M TMAO are adopted in this study. The unfolding transitions and folded conformations of the three SNase fragments were detected by far- and near-ultraviolet circular dichroism and intrinsic tryptophan fluorescence measurements. The tertiary structures and internal motions of the fragments were determined by NMR spectroscopy. Both G-88W and V-66W single mutations as well as a small organic osmolyte (Trimethylamine N-oxide, TMAO) can fold the fragment into a native-like conformation. However, the tertiary structures of the three fragments exhibit different degrees of folding stability and compactness. G-88W110 adopts a relatively rigid structure representing a most stable native-like beta-subdomain conformation of the three fragments. V-66W110- and TMAO-stabilized SNase110 produce less compact structures having a less stable "beta-barrel" structural region. The different folding status accounts for the different backbone dynamic and urea-unfolding transition features of the three fragments. The G-20I/G-29I-mutant variants of the three fragments have provided the evidence that the folding status is correlated closely to the packing of the beta-strands in the beta-barrel of the fragments. The native-like beta-barrel structural region acts as a nonlocal nucleus for folding the fragment. The tertiary folding of the three fragments is initiated by formation of the local nucleation sites at two beta-turn regions, I-18-D-21 and Y-27-Q-30, and developed by the formation of a nonlocal nucleation site at the beta-barrel region. The formation of beta-barrel and overall structure is concerted, but the level of cooperativity is different for the three 1-110 residues SNase fragments.
About this Structure
1RKN is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.
Reference
Folding stability and cooperativity of the three forms of 1-110 residues fragment of staphylococcal nuclease., Xie T, Liu D, Feng Y, Shan L, Wang J, Biophys J. 2007 Mar 15;92(6):2090-107. Epub 2006 Dec 15. PMID:17172296
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