1j54
From Proteopedia
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|PDB= 1j54 |SIZE=350|CAPTION= <scene name='initialview01'>1j54</scene>, resolution 1.7Å | |PDB= 1j54 |SIZE=350|CAPTION= <scene name='initialview01'>1j54</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TMP:THYMIDINE-5'-PHOSPHATE'>TMP</scene> | + | |LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=TMP:THYMIDINE-5'-PHOSPHATE'>TMP</scene> |
| - | + | |ACTIVITY= <span class='plainlinks'>[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] </span> | |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1j53|1J53]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1j54 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1j54 OCA], [http://www.ebi.ac.uk/pdbsum/1j54 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1j54 RCSB]</span> | ||
}} | }} | ||
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[[Category: Hamdan, S.]] | [[Category: Hamdan, S.]] | ||
[[Category: Ollis, D L.]] | [[Category: Ollis, D L.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: MN]] | ||
| - | [[Category: TMP]] | ||
[[Category: dna polymerase proofreading domain]] | [[Category: dna polymerase proofreading domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:28:59 2008'' |
Revision as of 18:29, 30 March 2008
| |||||||
| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Activity: | DNA-directed DNA polymerase, with EC number 2.7.7.7 | ||||||
| Related: | 1J53
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Structure of the N-terminal exonuclease domain of the epsilon subunit of E.coli DNA polymerase III at pH 5.8
Overview
The epsilon subunit of the Escherichia coli replicative DNA polymerase III is the proofreading 3'-5' exonuclease. Structures of its catalytic N-terminal domain (epsilon186) were determined at two pH values (5.8 and 8.5) at resolutions of 1.7-1.8 A, in complex with two Mn(II) ions and a nucleotide product of its reaction, thymidine 5'-monophosphate. The protein structure is built around a core five-stranded beta sheet that is a common feature of members of the DnaQ superfamily. The structures were identical, except for differences in the way TMP and water molecules are coordinated to the binuclear metal center in the active site. These data are used to develop a mechanism for epsilon and to produce a plausible model of the complex of epsilon186 with DNA.
About this Structure
1J54 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
Reference
Structural basis for proofreading during replication of the Escherichia coli chromosome., Hamdan S, Carr PD, Brown SE, Ollis DL, Dixon NE, Structure. 2002 Apr;10(4):535-46. PMID:11937058
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