1je5

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(New page: 200px<br /><applet load="1je5" size="450" color="white" frame="true" align="right" spinBox="true" caption="1je5, resolution 1.90&Aring;" /> '''Crystal Structure of...)
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[[Image:1je5.jpg|left|200px]]<br /><applet load="1je5" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1je5.jpg|left|200px]]<br /><applet load="1je5" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1je5, resolution 1.90&Aring;" />
caption="1je5, resolution 1.90&Aring;" />
'''Crystal Structure of gp2.5, a Single-Stranded DNA Binding Protein Encoded by Bacteriophage T7'''<br />
'''Crystal Structure of gp2.5, a Single-Stranded DNA Binding Protein Encoded by Bacteriophage T7'''<br />
==Overview==
==Overview==
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The gene 2.5 protein (gp2.5) of bacteriophage T7 is a single-stranded DNA, (ssDNA) binding protein that has essential roles in DNA replication and, recombination. In addition to binding DNA, gp2.5 physically interacts with, T7 DNA polymerase and T7 primase-helicase during replication to coordinate, events at the replication fork. We have determined a 1.9-A crystal, structure of gp2.5 and show that it has a conserved OB-fold, (oligosaccharide/oligonucleotide binding fold) that is well adapted for, interactions with ssDNA. Superposition of the OB-folds of gp2.5 and other, ssDNA binding proteins reveals a conserved patch of aromatic residues that, stack against the bases of ssDNA in the other crystal structures, suggesting that gp2.5 binds to ssDNA in a similar manner. An acidic, C-terminal extension of the gp2.5 protein, which is required for dimer, formation and for interactions with the T7 DNA polymerase and the, primase-helicase, appears to be flexible and may act as a switch that, modulates the DNA binding affinity of gp2.5.
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The gene 2.5 protein (gp2.5) of bacteriophage T7 is a single-stranded DNA (ssDNA) binding protein that has essential roles in DNA replication and recombination. In addition to binding DNA, gp2.5 physically interacts with T7 DNA polymerase and T7 primase-helicase during replication to coordinate events at the replication fork. We have determined a 1.9-A crystal structure of gp2.5 and show that it has a conserved OB-fold (oligosaccharide/oligonucleotide binding fold) that is well adapted for interactions with ssDNA. Superposition of the OB-folds of gp2.5 and other ssDNA binding proteins reveals a conserved patch of aromatic residues that stack against the bases of ssDNA in the other crystal structures, suggesting that gp2.5 binds to ssDNA in a similar manner. An acidic C-terminal extension of the gp2.5 protein, which is required for dimer formation and for interactions with the T7 DNA polymerase and the primase-helicase, appears to be flexible and may act as a switch that modulates the DNA binding affinity of gp2.5.
==About this Structure==
==About this Structure==
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1JE5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t7 Bacteriophage t7] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JE5 OCA].
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1JE5 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteriophage_t7 Bacteriophage t7] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JE5 OCA].
==Reference==
==Reference==
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[[Category: Bacteriophage t7]]
[[Category: Bacteriophage t7]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Ellenberger, T.E.]]
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[[Category: Ellenberger, T E.]]
[[Category: Hollis, T.]]
[[Category: Hollis, T.]]
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[[Category: Richardson, C.C.]]
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[[Category: Richardson, C C.]]
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[[Category: Stattel, J.M.]]
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[[Category: Stattel, J M.]]
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[[Category: Walther, D.S.]]
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[[Category: Walther, D S.]]
[[Category: CA]]
[[Category: CA]]
[[Category: beta barrel]]
[[Category: beta barrel]]
[[Category: ob-fold]]
[[Category: ob-fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:09:22 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:36 2008''

Revision as of 11:21, 21 February 2008


1je5, resolution 1.90Å

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Crystal Structure of gp2.5, a Single-Stranded DNA Binding Protein Encoded by Bacteriophage T7

Overview

The gene 2.5 protein (gp2.5) of bacteriophage T7 is a single-stranded DNA (ssDNA) binding protein that has essential roles in DNA replication and recombination. In addition to binding DNA, gp2.5 physically interacts with T7 DNA polymerase and T7 primase-helicase during replication to coordinate events at the replication fork. We have determined a 1.9-A crystal structure of gp2.5 and show that it has a conserved OB-fold (oligosaccharide/oligonucleotide binding fold) that is well adapted for interactions with ssDNA. Superposition of the OB-folds of gp2.5 and other ssDNA binding proteins reveals a conserved patch of aromatic residues that stack against the bases of ssDNA in the other crystal structures, suggesting that gp2.5 binds to ssDNA in a similar manner. An acidic C-terminal extension of the gp2.5 protein, which is required for dimer formation and for interactions with the T7 DNA polymerase and the primase-helicase, appears to be flexible and may act as a switch that modulates the DNA binding affinity of gp2.5.

About this Structure

1JE5 is a Single protein structure of sequence from Bacteriophage t7 with as ligand. Full crystallographic information is available from OCA.

Reference

Structure of the gene 2.5 protein, a single-stranded DNA binding protein encoded by bacteriophage T7., Hollis T, Stattel JM, Walther DS, Richardson CC, Ellenberger T, Proc Natl Acad Sci U S A. 2001 Aug 14;98(17):9557-62. Epub 2001 Jul 31. PMID:11481454

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