1j3e

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|PDB= 1j3e |SIZE=350|CAPTION= <scene name='initialview01'>1j3e</scene>, resolution 2.5&Aring;
|PDB= 1j3e |SIZE=350|CAPTION= <scene name='initialview01'>1j3e</scene>, resolution 2.5&Aring;
|SITE=
|SITE=
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|LIGAND=
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|LIGAND= <scene name='pdbligand=6MA:N6-METHYL-DEOXY-ADENOSINE-5&#39;-MONOPHOSPHATE'>6MA</scene>, <scene name='pdbligand=DA:2&#39;-DEOXYADENOSINE-5&#39;-MONOPHOSPHATE'>DA</scene>, <scene name='pdbligand=DC:2&#39;-DEOXYCYTIDINE-5&#39;-MONOPHOSPHATE'>DC</scene>, <scene name='pdbligand=DG:2&#39;-DEOXYGUANOSINE-5&#39;-MONOPHOSPHATE'>DG</scene>, <scene name='pdbligand=DT:THYMIDINE-5&#39;-MONOPHOSPHATE'>DT</scene>
|ACTIVITY=
|ACTIVITY=
|GENE= SeqA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
|GENE= SeqA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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|DOMAIN=
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|RELATEDENTRY=[[1iu3|1IU3]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j3e OCA], [http://www.ebi.ac.uk/pdbsum/1j3e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j3e RCSB]</span>
}}
}}
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[[Category: structural genomic]]
[[Category: structural genomic]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:58:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:28:20 2008''

Revision as of 18:28, 30 March 2008

Image:1j3e.gif


PDB ID 1j3e

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands: , , , ,
Gene: SeqA (Escherichia coli)
Related: 1IU3


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of the E.coli SeqA protein complexed with N6-methyladenine- guanine mismatch DNA


Overview

The Escherichia coli SeqA protein recognizes the 11 hemimethylated G-mA-T-C sites in the oriC region of the chromosome, and prevents replication over-initiation within one cell cycle. The crystal structure of the SeqA C-terminal domain with hemimethylated DNA revealed the N6-methyladenine recognition mechanism; however, the mechanism of discrimination between the hemimethylated and fully methylated states has remained elusive. In the present study, we performed mutational analyses of hemimethylated G-mA-T-C sequences with the minimal DNA-binding domain of SeqA (SeqA71-181), and found that SeqA71-181 specifically binds to hemimethylated DNA containing a sequence with a mismatched mA:G base pair [G-mA(:G)-T-C] as efficiently as the normal hemimethylated G-mA(:T)-T-C sequence. We determined the crystal structures of SeqA71-181 complexed with the mismatched and normal hemimethylated DNAs at 2.5 and 3.0 A resolutions, respectively, and found that the mismatched mA:G base pair and the normal mA:T base pair are recognized by SeqA in a similar manner. Furthermore, in both crystal structures, an electron density is present near the unmethylated adenine, which is only methylated in the fully methylated state. This electron density, which may be due to a water molecule or a metal ion, can exist in the hemimethylated state, but not in the fully methylated state, because of steric clash with the additional methyl group.

About this Structure

1J3E is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structural and biochemical analyses of hemimethylated DNA binding by the SeqA protein., Fujikawa N, Kurumizaka H, Nureki O, Tanaka Y, Yamazoe M, Hiraga S, Yokoyama S, Nucleic Acids Res. 2004 Jan 2;32(1):82-92. Print 2004. PMID:14704346

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