1kjk: Difference between revisions
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'''Solution structure of the lambda integrase amino-terminal domain'''<br /> | '''Solution structure of the lambda integrase amino-terminal domain'''<br /> | ||
==Overview== | ==Overview== | ||
The integrase protein (Int) from bacteriophage lambda catalyzes the | The integrase protein (Int) from bacteriophage lambda catalyzes the insertion and excision of the viral genome into and out of Escherichia coli. It is a member of the lambda-Int family of site-specific recombinases that catalyze a diverse array of DNA rearrangements in archaebacteria, eubacteria, and yeast and belongs to the subset of this family that possesses two autonomous DNA-binding domains. The heterobivalent properties of Int can be decomposed into a carboxyl-terminal domain that executes the DNA cleavage and ligation reactions and a smaller amino-terminal domain that binds to an array of conserved DNA sites within the phage arms, thereby arranging Int protomers within the higher-order recombinogenic complex. We have determined that residues Met-1 to Leu-64 of Int constitute the minimal arm-type DNA-binding domain (INT-DBD(1-64)) and solved the solution structure by using NMR. We show that the INT-DBD(1-64) is a novel member of the growing family of three-stranded beta-sheet DNA-binding proteins, because it supplements this motif with a disordered amino-terminal basic tail that is important for arm-site binding. A model of the arm-DNA-binding domain recognizing its cognate DNA site is proposed on the basis of similarities with the analogous domain of Tn916 Int and is discussed in relation to other features of the protein. | ||
==About this Structure== | ==About this Structure== | ||
1KJK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda]. Full crystallographic information is available from [http:// | 1KJK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_lambda Enterobacteria phage lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KJK OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Enterobacteria phage lambda]] | [[Category: Enterobacteria phage lambda]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Clubb, R | [[Category: Clubb, R T.]] | ||
[[Category: Landy, A.]] | [[Category: Landy, A.]] | ||
[[Category: Sarkar, D.]] | [[Category: Sarkar, D.]] | ||
[[Category: Wojciak, J | [[Category: Wojciak, J M.]] | ||
[[Category: dna recombination]] | [[Category: dna recombination]] | ||
[[Category: dna-binding domain]] | [[Category: dna-binding domain]] | ||
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[[Category: three-stranded beta-sheet]] | [[Category: three-stranded beta-sheet]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:34:49 2008'' | ||
Revision as of 14:34, 21 February 2008
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Solution structure of the lambda integrase amino-terminal domain
OverviewOverview
The integrase protein (Int) from bacteriophage lambda catalyzes the insertion and excision of the viral genome into and out of Escherichia coli. It is a member of the lambda-Int family of site-specific recombinases that catalyze a diverse array of DNA rearrangements in archaebacteria, eubacteria, and yeast and belongs to the subset of this family that possesses two autonomous DNA-binding domains. The heterobivalent properties of Int can be decomposed into a carboxyl-terminal domain that executes the DNA cleavage and ligation reactions and a smaller amino-terminal domain that binds to an array of conserved DNA sites within the phage arms, thereby arranging Int protomers within the higher-order recombinogenic complex. We have determined that residues Met-1 to Leu-64 of Int constitute the minimal arm-type DNA-binding domain (INT-DBD(1-64)) and solved the solution structure by using NMR. We show that the INT-DBD(1-64) is a novel member of the growing family of three-stranded beta-sheet DNA-binding proteins, because it supplements this motif with a disordered amino-terminal basic tail that is important for arm-site binding. A model of the arm-DNA-binding domain recognizing its cognate DNA site is proposed on the basis of similarities with the analogous domain of Tn916 Int and is discussed in relation to other features of the protein.
About this StructureAbout this Structure
1KJK is a Single protein structure of sequence from Enterobacteria phage lambda. Full crystallographic information is available from OCA.
ReferenceReference
Arm-site binding by lambda -integrase: solution structure and functional characterization of its amino-terminal domain., Wojciak JM, Sarkar D, Landy A, Clubb RT, Proc Natl Acad Sci U S A. 2002 Mar 19;99(6):3434-9. PMID:11904406
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