2f3v: Difference between revisions

|PDB= 2f3v |SIZE=350|CAPTION= <scene name='initialview01'>2f3v</scene>

|SITE=  

|LIGAND=  

|ACTIVITY= <span class='plainlinks'>[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] </span>

|GENE=  

|RELATEDENTRY=[[2f3w|2F3W]], [[1rkn|1RKN]]

|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2f3v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f3v OCA], [http://www.ebi.ac.uk/pdbsum/2f3v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2f3v RCSB]</span>

'''Solution structure of 1-110 fragment of staphylococcal nuclease with V66W 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==

2F3V 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=2F3V OCA].

 

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: Single protein]]

[[Category: Feng, Y.]]

[[Category: Liu, D.]]

[[Category: Shan, L.]]

[[Category: Wang, J.]]

[[Category: Xie, T.]]

[[Category: Ye, K.]]