1n4j: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1n4j.gif|left|200px]] | [[Image:1n4j.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1n4j", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
--> | |||
{{STRUCTURE_1n4j| PDB=1n4j | SCENE= }} | |||
}} | |||
'''STREPTAVIDIN MUTANT N23A AT 2.18A''' | '''STREPTAVIDIN MUTANT N23A AT 2.18A''' | ||
| Line 31: | Line 28: | ||
[[Category: Stenkamp, R E.]] | [[Category: Stenkamp, R E.]] | ||
[[Category: Trong, I Le.]] | [[Category: Trong, I Le.]] | ||
[[Category: | [[Category: Homotetramer]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:05:12 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 02:05, 3 May 2008
STREPTAVIDIN MUTANT N23A AT 2.18A
OverviewOverview
An elaborate hydrogen-bonding network contributes to the tight binding of biotin to streptavidin. The specific energetic contributions of hydrogen bonds to the biotin ureido oxygen have previously been investigated by mapping the equilibrium and activation thermodynamic signatures of N23A, N23E, S27A, Y43A and Y43F site-directed mutants [Klumb et al. (1998), Biochemistry, 37, 7657-7663]. The crystal structures of these variants in the unbound and biotin-bound states provide structural insight into the energetic alterations and are described here. High (1.5-2.2 A) to atomic resolution (1.14 A) structures were obtained and structural models were refined to R values ranging from 0.12 to 0.20. The overall folding of streptavidin as described previously has not changed in any of the mutant structures. Major deviations such as side-chain shifts of residues in the binding site are observed only for the N23A and Y43A mutations. In none of the mutants is a systematic shift of biotin observed when one of the hydrogen-bonding partners to the ureido oxygen of biotin is removed. Recent thermodynamic studies report increases of DeltaDeltaG(o) of 5.0-14.6 kJ mol(-1) for these mutants with respect to the wild-type protein. The decreasing stabilities of the complexes of the mutants are discussed in terms of their structures.
About this StructureAbout this Structure
1N4J is a Single protein structure of sequence from Streptomyces avidinii. Full crystallographic information is available from OCA.
ReferenceReference
Structural studies of hydrogen bonds in the high-affinity streptavidin-biotin complex: mutations of amino acids interacting with the ureido oxygen of biotin., Le Trong I, Freitag S, Klumb LA, Chu V, Stayton PS, Stenkamp RE, Acta Crystallogr D Biol Crystallogr. 2003 Sep;59(Pt 9):1567-73. Epub 2003, Aug 19. PMID:12925786 Page seeded by OCA on Sat May 3 02:05:12 2008