1fxx: Difference between revisions

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[[Image:1fxx.jpg|left|200px]]


{{Structure
==THE STRUCTURE OF EXONUCLEASE I SUGGESTS HOW PROCESSIVITY IS ACHIEVED==
|PDB= 1fxx |SIZE=350|CAPTION= <scene name='initialview01'>1fxx</scene>, resolution 2.4&Aring;
<StructureSection load='1fxx' size='340' side='right'caption='[[1fxx]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>
<table><tr><td colspan='2'>[[1fxx]] is a 1 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FXX FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[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] </span>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fxx OCA], [https://pdbe.org/1fxx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fxx RCSB], [https://www.ebi.ac.uk/pdbsum/1fxx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fxx ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fxx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fxx OCA], [http://www.ebi.ac.uk/pdbsum/1fxx PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fxx RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/EX1_ECOLI EX1_ECOLI] Also functions as a DNA deoxyribophosphodiesterase that releases deoxyribose-phosphate moieties following the cleavage DNA at an apurinic/apyrimidinic (AP) site by either an AP endonuclease AP lyase.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fx/1fxx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fxx ConSurf].
<div style="clear:both"></div>


'''THE STRUCTURE OF EXONUCLEASE I SUGGESTS HOW PROCESSIVITY IS ACHIEVED'''
==See Also==
 
*[[Exonuclease|Exonuclease]]
 
*[[Exonuclease 3D structures|Exonuclease 3D structures]]
==Overview==
__TOC__
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.
</StructureSection>
 
==About this Structure==
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==
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: Large Structures]]
[[Category: Single protein]]
[[Category: Breyer WA]]
[[Category: Breyer, W A.]]
[[Category: Matthews BW]]
[[Category: Matthews, B W.]]
[[Category: alpha-beta domain]]
[[Category: dnaq superfamily]]
[[Category: sh3-like domain]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:32:30 2008''

Latest revision as of 10:20, 7 February 2024

THE STRUCTURE OF EXONUCLEASE I SUGGESTS HOW PROCESSIVITY IS ACHIEVEDTHE STRUCTURE OF EXONUCLEASE I SUGGESTS HOW PROCESSIVITY IS ACHIEVED

Structural highlights

1fxx is a 1 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.4Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

EX1_ECOLI Also functions as a DNA deoxyribophosphodiesterase that releases deoxyribose-phosphate moieties following the cleavage DNA at an apurinic/apyrimidinic (AP) site by either an AP endonuclease AP lyase.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

1fxx, resolution 2.40Å

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