1fxx

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[[Image:1fxx.jpg|left|200px]]<br /><applet load="1fxx" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fxx.jpg|left|200px]]
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caption="1fxx, resolution 2.4&Aring;" />
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'''THE STRUCTURE OF EXONUCLEASE I SUGGESTS HOW PROCESSIVITY IS ACHIEVED'''<br />
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{{Structure
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|PDB= 1fxx |SIZE=350|CAPTION= <scene name='initialview01'>1fxx</scene>, resolution 2.4&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Exodeoxyribonuclease_I Exodeoxyribonuclease I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.1 3.1.11.1]
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|GENE=
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}}
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'''THE STRUCTURE OF EXONUCLEASE I SUGGESTS HOW PROCESSIVITY IS ACHIEVED'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1FXX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=PO4:'>PO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Exodeoxyribonuclease_I Exodeoxyribonuclease I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.11.1 3.1.11.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXX OCA].
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1FXX is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FXX OCA].
==Reference==
==Reference==
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Structure of Escherichia coli exonuclease I suggests how processivity is achieved., Breyer WA, Matthews BW, Nat Struct Biol. 2000 Dec;7(12):1125-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11101894 11101894]
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Structure of Escherichia coli exonuclease I suggests how processivity is achieved., Breyer WA, Matthews BW, Nat Struct Biol. 2000 Dec;7(12):1125-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11101894 11101894]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Exodeoxyribonuclease I]]
[[Category: Exodeoxyribonuclease I]]
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[[Category: sh3-like domain]]
[[Category: sh3-like domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:15:25 2008''

Revision as of 09:15, 20 March 2008


PDB ID 1fxx

Drag the structure with the mouse to rotate
, resolution 2.4Å
Ligands: , and
Activity: Exodeoxyribonuclease I, with EC number 3.1.11.1
Coordinates: save as pdb, mmCIF, xml



THE STRUCTURE OF EXONUCLEASE I SUGGESTS HOW PROCESSIVITY IS ACHIEVED


Overview

Exonuclease I (ExoI) from Escherichia coli is a monomeric enzyme that processively degrades single stranded DNA in the 3' to 5' direction and has been implicated in DNA recombination and repair. Determination of the structure of ExoI to 2.4 A resolution using X-ray crystallography verifies the expected correspondence between a region of ExoI and the exonuclease (or proofreading) domains of the DNA polymerases. The overall fold of ExoI also includes two other regions, one of which extends the exonuclease domain and another that can be described as an elaborated SH3 domain. These three regions combine to form a molecule that is shaped like the letter C, although it also contains a segment that effectively converts the C into an O-like shape. The structure of ExoI thus provides additional support for the idea that DNA metabolizing enzymes achieve processivity by completely enclosing the DNA.

About this Structure

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

Reference

Structure of Escherichia coli exonuclease I suggests how processivity is achieved., Breyer WA, Matthews BW, Nat Struct Biol. 2000 Dec;7(12):1125-8. PMID:11101894

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