1rxj: Difference between revisions

Revision as of 23:45, 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:1rxj.png

Template:STRUCTURE 1rxj

Crystal structure of streptavidin mutant (M2) where the L3,4 loop was replace by that of avidinCrystal structure of streptavidin mutant (M2) where the L3,4 loop was replace by that of avidin

Template:ABSTRACT PUBMED 15079055

About this StructureAbout this Structure

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

ReferenceReference

Structural elements responsible for conversion of streptavidin to a pseudoenzyme., Eisenberg-Domovich Y, Pazy Y, Nir O, Raboy B, Bayer EA, Wilchek M, Livnah O, Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):5916-21. Epub 2004 Apr 12. PMID:15079055

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of streptavidin mutant (M2) where the L3,4 loop was replace by that of avidin'''
+===Crystal structure of streptavidin mutant (M2) where the L3,4 loop was replace by that of avidin===
-==Overview==
+<!--
-Avidin enhances the hydrolysis of biotinyl p-nitrophenyl ester (BNP) under mild alkaline conditions, whereas streptavidin prevents hydrolysis of BNP up to pH 12. Recently, we imposed hydrolytic activity on streptavidin by rational mutagenesis, based on the molecular elements responsible for the hydrolysis by avidin. Three mutants were designed, whereby the desired features, the distinctive L124R point mutation (M1), the L3,4 loop replacement (M2), and the combined mutation (M3), were transferred from avidin to streptavidin. The crystal structures of the mutants, in complex with biotinyl p-nitroanilide (BNA), the stable amide analogue of BNP, were determined. The results demonstrate that the point mutation alone has little effect on hydrolysis, and BNA exhibits a conformation similar to that of streptavidin. Substitution of a lengthier L3,4 loop (from avidin to streptavidin), resulted in an open conformation, thus exposing the ligand to solvent. Moreover, the amide bond of BNA was flipped relative to that of the streptavidin and M1 complexes, thus deflecting the nitro group toward Lys-121. Consequently, the leaving group potential of the nitrophenyl group of BNP is increased, and M2 hydrolyzes BNP at pH values &gt;8.5. To better emulate the hydrolytic potential of avidin, M3 was required. The combination of loop replacement and point mutation served to further increase the leaving group potential by interaction of the nitro group with Arg-124 and Lys-121. The information derived from this study may provide insight into the design of enzymes and transfer of desired properties among homologous proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_15079055}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15079055 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15079055}}
 ==About this Structure==
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 [[Category: Pseudo enzymatic activity]]
 [[Category: Streptavidin]]
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