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| - | [[Image:2of8.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2of8| PDB=2of8 | SCENE= }} | | {{STRUCTURE_2of8| PDB=2of8 | SCENE= }} |
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| - | '''Crystal structure of AVR4 (D39A/C122S)-BNA complex'''
| + | ===Crystal structure of AVR4 (D39A/C122S)-BNA complex=== |
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| - | ==Overview==
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| - | The homotetrameric and biotin-binding properties of avidin and streptavidin have been exploited for a myriad of biotechnological applications and theoretical studies. Among the few differences between the two proteins is the capacity of avidin to hydrolyze biotinyl p-nitrophenyl ester (BNP), as opposed to streptavidin, which fully protects the same pseudosubstrate from hydrolysis. Combined mutagenesis and X-ray analysis have been used to attempt to understand this diametric difference in activities. It was found that a charged residue and one of the loops (L3,4) are together responsible for this difference. Recently, the avidin-related analogue AVR4 was found to have an even more pronounced BNP-hydrolysis activity than avidin. Again, the combination of charged residue(s) (Asp39 and/or Arg112) and the rigid conformation of the L3,4 loop was suggested to be responsible for the observed hydrolysis reaction. However, replacement of the latter charged residues in AVR4 resulted in only a modest reduction in hydrolytic activity at most, whereas replacement of the L3,4 loop of avidin with the rigid loop of AVR4 caused a dramatic increase in the activity of avidin. These results clearly demonstrate that the main feature responsible for the observed differences in rates of hydrolysis among the avidins is the conformational status of the L3,4 loop, which imposes conformational constraints on the pseudosubstrate, thereby rendering it susceptible to nucleophilic attack by solvent. In this context, the hydrolytic properties of the avidins reflect enzyme catalysis, in that subtleties in substrate binding are the determining features of catalytic efficiency. | + | The line below this paragraph, {{ABSTRACT_PUBMED_18323625}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 18323625 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_18323625}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pseudo-catalysis]] | | [[Category: Pseudo-catalysis]] |
| | [[Category: Streptavidin]] | | [[Category: Streptavidin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 24 09:25:34 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:27:46 2008'' |
Revision as of 09:27, 28 July 2008
Template:STRUCTURE 2of8
Crystal structure of AVR4 (D39A/C122S)-BNA complex
Template:ABSTRACT PUBMED 18323625
About this Structure
2OF8 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Critical importance of loop conformation to avidin-enhanced hydrolysis of an active biotin ester., Hayouka R, Eisenberg-Domovich Y, Hytonen VP, Maatta JA, Nordlund HR, Kulomaa MS, Wilchek M, Bayer EA, Livnah O, Acta Crystallogr D Biol Crystallogr. 2008 Mar;64(Pt 3):302-8. Epub 2008, Feb 20. PMID:18323625
Page seeded by OCA on Mon Jul 28 12:27:46 2008
