1pvq: Difference between revisions
New page: left|200px<br /><applet load="1pvq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pvq, resolution 2.75Å" /> '''BASIS FOR A SWITCH I... |
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[[Image:1pvq.gif|left|200px]]<br /><applet load="1pvq" size=" | [[Image:1pvq.gif|left|200px]]<br /><applet load="1pvq" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1pvq, resolution 2.75Å" /> | caption="1pvq, resolution 2.75Å" /> | ||
'''BASIS FOR A SWITCH IN SUBSTRATE SPECIFICITY: CRYSTAL STRUCTURE OF SELECTED VARIANT OF CRE SITE-SPECIFIC RECOMBINASE, LNSGG BOUND TO THE ENGINEERED RECOGNITION SITE LOXM7'''<br /> | '''BASIS FOR A SWITCH IN SUBSTRATE SPECIFICITY: CRYSTAL STRUCTURE OF SELECTED VARIANT OF CRE SITE-SPECIFIC RECOMBINASE, LNSGG BOUND TO THE ENGINEERED RECOGNITION SITE LOXM7'''<br /> | ||
==Overview== | ==Overview== | ||
The basis for the altered DNA specificities of two Cre recombinase | The basis for the altered DNA specificities of two Cre recombinase variants, obtained by mutation and selection, was revealed by their cocrystal structures. The proteins share similar substitutions but differ in their preferences for the natural LoxP substrate and an engineered substrate that is inactive with wild-type Cre, LoxM7. One variant preferentially recombines LoxM7 and contacts the substituted bases through a hydrated network of novel interlocking protein-DNA contacts. The other variant recognizes both LoxP and LoxM7 utilizing the same DNA backbone contact but different base contacts, facilitated by an unexpected DNA shift. Assisted by water, novel interaction networks can arise from few protein substitutions, suggesting how new DNA binding specificities might evolve. The contributions of macromolecular plasticity and water networks in specific DNA recognition observed here present a challenge for predictive schemes. | ||
==About this Structure== | ==About this Structure== | ||
1PVQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p21 Enterobacteria phage p21]. Full crystallographic information is available from [http:// | 1PVQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Enterobacteria_phage_p21 Enterobacteria phage p21]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PVQ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Abel, J.]] | [[Category: Abel, J.]] | ||
[[Category: Baldwin, E | [[Category: Baldwin, E P.]] | ||
[[Category: Gelato, K | [[Category: Gelato, K A.]] | ||
[[Category: Kim, H.]] | [[Category: Kim, H.]] | ||
[[Category: Martin, S | [[Category: Martin, S S.]] | ||
[[Category: Santoro, S | [[Category: Santoro, S W.]] | ||
[[Category: Schultz, P | [[Category: Schultz, P G.]] | ||
[[Category: cre]] | [[Category: cre]] | ||
[[Category: cre-loxp recombination]] | [[Category: cre-loxp recombination]] | ||
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[[Category: recombinase]] | [[Category: recombinase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:32:59 2008'' | ||
Revision as of 15:33, 21 February 2008
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BASIS FOR A SWITCH IN SUBSTRATE SPECIFICITY: CRYSTAL STRUCTURE OF SELECTED VARIANT OF CRE SITE-SPECIFIC RECOMBINASE, LNSGG BOUND TO THE ENGINEERED RECOGNITION SITE LOXM7
OverviewOverview
The basis for the altered DNA specificities of two Cre recombinase variants, obtained by mutation and selection, was revealed by their cocrystal structures. The proteins share similar substitutions but differ in their preferences for the natural LoxP substrate and an engineered substrate that is inactive with wild-type Cre, LoxM7. One variant preferentially recombines LoxM7 and contacts the substituted bases through a hydrated network of novel interlocking protein-DNA contacts. The other variant recognizes both LoxP and LoxM7 utilizing the same DNA backbone contact but different base contacts, facilitated by an unexpected DNA shift. Assisted by water, novel interaction networks can arise from few protein substitutions, suggesting how new DNA binding specificities might evolve. The contributions of macromolecular plasticity and water networks in specific DNA recognition observed here present a challenge for predictive schemes.
About this StructureAbout this Structure
1PVQ is a Protein complex structure of sequences from Enterobacteria phage p21. Full crystallographic information is available from OCA.
ReferenceReference
A specificity switch in selected cre recombinase variants is mediated by macromolecular plasticity and water., Baldwin EP, Martin SS, Abel J, Gelato KA, Kim H, Schultz PG, Santoro SW, Chem Biol. 2003 Nov;10(11):1085-94. PMID:14652076
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