From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1nqm.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1nqm.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1nqm| PDB=1nqm | SCENE= }} | | {{STRUCTURE_1nqm| PDB=1nqm | SCENE= }} |
| | | | |
| - | '''Structure of Savm-W120K, streptavidin mutant'''
| + | ===Structure of Savm-W120K, streptavidin mutant=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The biotin-binding tetrameric proteins, streptavidin from Streptomyces avidinii and chicken egg white avidin, are excellent models for the study of subunit-subunit interactions of a multimeric protein. Efforts are thus being made to prepare mutated forms of streptavidin and avidin, which would form monomers or dimers, in order to examine their effect on quaternary structure and assembly. In the present communication, we compared the crystal structures of binding site W-->K mutations in streptavidin and avidin. In solution, both mutant proteins are known to form dimers, but upon crystallization, both formed tetramers with the same parameters as the native proteins. All of the intersubunit bonds were conserved, except for the hydrophobic interaction between biotin and the tryptophan that was replaced by lysine. In the crystal structure, the binding site of the mutated apo-avidin contains 3 molecules of structured water instead of the 5 contained in the native protein. The lysine side chain extends in a direction opposite that of the native tryptophan, the void being partially filled by an adjacent lysine residue. Nevertheless, the binding-site conformation observed for the mutant tetramer is an artificial consequence of crystal packing that would not be maintained in the solution-phase dimer. It appears that the dimer-tetramer transition may be concentration dependent, and the interaction among subunits obeys the law of mass action. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12837778}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12837778 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_12837778}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 34: |
Line 38: |
| | [[Category: Monomer-monomer interaction]] | | [[Category: Monomer-monomer interaction]] |
| | [[Category: Streptavidin]] | | [[Category: Streptavidin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:51:51 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 14:22:07 2008'' |
Revision as of 11:22, 27 July 2008
Template:STRUCTURE 1nqm
Structure of Savm-W120K, streptavidin mutant
Template:ABSTRACT PUBMED 12837778
About this Structure
1NQM is a Single protein structure of sequence from Streptomyces avidinii. Full crystallographic information is available from OCA.
Reference
Dimer-tetramer transition between solution and crystalline states of streptavidin and avidin mutants., Pazy Y, Eisenberg-Domovich Y, Laitinen OH, Kulomaa MS, Bayer EA, Wilchek M, Livnah O, J Bacteriol. 2003 Jul;185(14):4050-6. PMID:12837778
Page seeded by OCA on Sun Jul 27 14:22:07 2008
