2flp: Difference between revisions

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New page: left|200px<br /> <applet load="2flp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2flp, resolution 2.40Å" /> '''Binary complex of t...
 
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[[Image:2flp.gif|left|200px]]<br />
[[Image:2flp.gif|left|200px]]<br /><applet load="2flp" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="2flp" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="2flp, resolution 2.40&Aring;" />
caption="2flp, resolution 2.40&Aring;" />
'''Binary complex of the catalytic core of human DNA polymerase iota with DNA (template G)'''<br />
'''Binary complex of the catalytic core of human DNA polymerase iota with DNA (template G)'''<br />


==Overview==
==Overview==
Substrate-induced conformational change of the protein is the linchpin of, enzymatic reactions. Replicative DNA polymerases, for example, convert, from an open to a closed conformation in response to dNTP binding. Human, DNA polymerase-iota (hPoliota), a member of the Y family of DNA, polymerases, differs strikingly from other polymerases in its much higher, proficiency and fidelity for nucleotide incorporation opposite template, purines than opposite template pyrimidines. We present here a, crystallographic analysis of hPoliota binary complexes, which together, with the ternary complexes show that, contrary to replicative DNA, polymerases, the DNA, and not the polymerase, undergoes the primary, substrate-induced conformational change. The incoming dNTP "pushes", templates A and G from the anti to the syn conformation dictated by a, rigid hPoliota active site. Together, the structures posit a mechanism for, template selection wherein dNTP binding induces a conformational switch in, template purines for productive Hoogsteen base pairing.
Substrate-induced conformational change of the protein is the linchpin of enzymatic reactions. Replicative DNA polymerases, for example, convert from an open to a closed conformation in response to dNTP binding. Human DNA polymerase-iota (hPoliota), a member of the Y family of DNA polymerases, differs strikingly from other polymerases in its much higher proficiency and fidelity for nucleotide incorporation opposite template purines than opposite template pyrimidines. We present here a crystallographic analysis of hPoliota binary complexes, which together with the ternary complexes show that, contrary to replicative DNA polymerases, the DNA, and not the polymerase, undergoes the primary substrate-induced conformational change. The incoming dNTP "pushes" templates A and G from the anti to the syn conformation dictated by a rigid hPoliota active site. Together, the structures posit a mechanism for template selection wherein dNTP binding induces a conformational switch in template purines for productive Hoogsteen base pairing.


==About this Structure==
==About this Structure==
2FLP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2FLP OCA].  
2FLP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/DNA-directed_DNA_polymerase DNA-directed DNA polymerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.7 2.7.7.7] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FLP OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Aggarwal, A.K.]]
[[Category: Aggarwal, A K.]]
[[Category: Johnson, R.E.]]
[[Category: Johnson, R E.]]
[[Category: Nair, D.T.]]
[[Category: Nair, D T.]]
[[Category: Prakash, L.]]
[[Category: Prakash, L.]]
[[Category: Prakash, S.]]
[[Category: Prakash, S.]]
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[[Category: y-family]]
[[Category: y-family]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:07:10 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:22:41 2008''

Revision as of 18:22, 21 February 2008

File:2flp.gif


2flp, resolution 2.40Å

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Binary complex of the catalytic core of human DNA polymerase iota with DNA (template G)

OverviewOverview

Substrate-induced conformational change of the protein is the linchpin of enzymatic reactions. Replicative DNA polymerases, for example, convert from an open to a closed conformation in response to dNTP binding. Human DNA polymerase-iota (hPoliota), a member of the Y family of DNA polymerases, differs strikingly from other polymerases in its much higher proficiency and fidelity for nucleotide incorporation opposite template purines than opposite template pyrimidines. We present here a crystallographic analysis of hPoliota binary complexes, which together with the ternary complexes show that, contrary to replicative DNA polymerases, the DNA, and not the polymerase, undergoes the primary substrate-induced conformational change. The incoming dNTP "pushes" templates A and G from the anti to the syn conformation dictated by a rigid hPoliota active site. Together, the structures posit a mechanism for template selection wherein dNTP binding induces a conformational switch in template purines for productive Hoogsteen base pairing.

About this StructureAbout this Structure

2FLP is a Single protein structure of sequence from Homo sapiens. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.

ReferenceReference

An incoming nucleotide imposes an anti to syn conformational change on the templating purine in the human DNA polymerase-iota active site., Nair DT, Johnson RE, Prakash L, Prakash S, Aggarwal AK, Structure. 2006 Apr;14(4):749-55. PMID:16615915

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