1nqm: Difference between revisions

Revision as of 14:22, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1nqm.png

Template:STRUCTURE 1nqm

Structure of Savm-W120K, streptavidin mutantStructure of Savm-W120K, streptavidin mutant

Template:ABSTRACT PUBMED 12837778

About this StructureAbout this Structure

1NQM is a Single protein structure of sequence from Streptomyces avidinii. Full crystallographic information is available from OCA.

ReferenceReference

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

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OCA

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-[[Image:1nqm.gif|left|200px]]
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 {{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--&gt;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==
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 [[Category: Monomer-monomer interaction]]
 [[Category: Streptavidin]]
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