1l8q

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(New page: 200px<br /><applet load="1l8q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l8q, resolution 2.700&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1l8q.gif|left|200px]]<br /><applet load="1l8q" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1l8q.gif|left|200px]]<br /><applet load="1l8q" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1l8q, resolution 2.700&Aring;" />
caption="1l8q, resolution 2.700&Aring;" />
'''CRYSTAL STRUCTURE OF DNA REPLICATION INITIATION FACTOR'''<br />
'''CRYSTAL STRUCTURE OF DNA REPLICATION INITIATION FACTOR'''<br />
==Overview==
==Overview==
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The initiation of DNA replication is a key event in the cell cycle of all, organisms. In bacteria, replication initiation occurs at specific origin, sequences that are recognized and processed by an oligomeric complex of, the initiator protein DnaA. We have determined the structure of the, conserved core of the Aquifex aeolicus DnaA protein to 2.7 A resolution., The protein comprises an AAA+ nucleotide-binding fold linked through a, long, helical connector to an all-helical DNA-binding domain. The, structure serves as a template for understanding the physical consequences, of a variety of DnaA mutations, and conserved motifs in the protein, suggest how two critical aspects of origin processing, DNA binding and, homo-oligomerization, are mediated. The spatial arrangement of these, motifs in DnaA is similar to that of the eukaryotic-like archaeal, replication initiation factor Cdc6/Orc1, demonstrating that mechanistic, elements of origin processing may be conserved across bacterial, archaeal, and eukaryotic domains of life.
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The initiation of DNA replication is a key event in the cell cycle of all organisms. In bacteria, replication initiation occurs at specific origin sequences that are recognized and processed by an oligomeric complex of the initiator protein DnaA. We have determined the structure of the conserved core of the Aquifex aeolicus DnaA protein to 2.7 A resolution. The protein comprises an AAA+ nucleotide-binding fold linked through a long, helical connector to an all-helical DNA-binding domain. The structure serves as a template for understanding the physical consequences of a variety of DnaA mutations, and conserved motifs in the protein suggest how two critical aspects of origin processing, DNA binding and homo-oligomerization, are mediated. The spatial arrangement of these motifs in DnaA is similar to that of the eukaryotic-like archaeal replication initiation factor Cdc6/Orc1, demonstrating that mechanistic elements of origin processing may be conserved across bacterial, archaeal and eukaryotic domains of life.
==About this Structure==
==About this Structure==
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1L8Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with MG and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L8Q OCA].
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1L8Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L8Q OCA].
==Reference==
==Reference==
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[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Berger, J.M.]]
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[[Category: Berger, J M.]]
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[[Category: Erzberger, J.P.]]
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[[Category: Erzberger, J P.]]
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[[Category: Pirruccello, M.M.]]
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[[Category: Pirruccello, M M.]]
[[Category: ADP]]
[[Category: ADP]]
[[Category: MG]]
[[Category: MG]]
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[[Category: replication initiation]]
[[Category: replication initiation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:22:39 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:32 2008''

Revision as of 11:42, 21 February 2008


1l8q, resolution 2.700Å

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CRYSTAL STRUCTURE OF DNA REPLICATION INITIATION FACTOR

Overview

The initiation of DNA replication is a key event in the cell cycle of all organisms. In bacteria, replication initiation occurs at specific origin sequences that are recognized and processed by an oligomeric complex of the initiator protein DnaA. We have determined the structure of the conserved core of the Aquifex aeolicus DnaA protein to 2.7 A resolution. The protein comprises an AAA+ nucleotide-binding fold linked through a long, helical connector to an all-helical DNA-binding domain. The structure serves as a template for understanding the physical consequences of a variety of DnaA mutations, and conserved motifs in the protein suggest how two critical aspects of origin processing, DNA binding and homo-oligomerization, are mediated. The spatial arrangement of these motifs in DnaA is similar to that of the eukaryotic-like archaeal replication initiation factor Cdc6/Orc1, demonstrating that mechanistic elements of origin processing may be conserved across bacterial, archaeal and eukaryotic domains of life.

About this Structure

1L8Q is a Single protein structure of sequence from Aquifex aeolicus with and as ligands. Full crystallographic information is available from OCA.

Reference

The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation., Erzberger JP, Pirruccello MM, Berger JM, EMBO J. 2002 Sep 16;21(18):4763-73. PMID:12234917

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