2g7e: Difference between revisions

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[[Image:2g7e.jpg|left|200px]]


{{Structure
==The 1.6 A crystal structure of Vibrio cholerae extracellular endonuclease I==
|PDB= 2g7e |SIZE=350|CAPTION= <scene name='initialview01'>2g7e</scene>, resolution 1.600&Aring;
<StructureSection load='2g7e' size='340' side='right'caption='[[2g7e]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>
<table><tr><td colspan='2'>[[2g7e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G7E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2G7E FirstGlance]. <br>
|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Deoxyribonuclease_I Deoxyribonuclease I], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.21.1 3.1.21.1] </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]] 1.6&#8491;</td></tr>
|GENE= EndA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 Vibrio cholerae])
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=2g7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g7e OCA], [https://pdbe.org/2g7e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2g7e RCSB], [https://www.ebi.ac.uk/pdbsum/2g7e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2g7e ProSAT]</span></td></tr>
|RELATEDENTRY=[[2g7f|2G7F]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2g7e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g7e OCA], [http://www.ebi.ac.uk/pdbsum/2g7e PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2g7e RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/Q2XSK9_VIBCL Q2XSK9_VIBCL]
== 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/g7/2g7e_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=2g7e ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The crystal structure of a periplasmic/extracellular endonuclease from Vibrio cholerae has been solved at low and at neutral pH. Crystals grown at pH 4.6 and 6.9 diffracted to 1.6 A (on BM01A at the ESRF) and 1.95 A (on a rotating-anode generator), respectively. The structures of the endonuclease were compared with the structure of a homologous enzyme in V. vulnificus. The structures of the V. cholerae enzyme at different pH values are essentially identical to each other and to the V. vulnificus enzyme. However, interesting features were observed in the solvent structures. Both V. cholerae structures reveal the presence of a chloride ion completely buried within the core of the protein, with the nearest solvent molecule approximately 7 A away. Magnesium, which is essential for catalysis, is present in the structure at neutral pH, but is absent at low pH, and may partly explain the inactivity of the enzyme at lower pH.


'''The 1.6 A crystal structure of Vibrio cholerae extracellular endonuclease I'''
The structure of Vibrio cholerae extracellular endonuclease I reveals the presence of a buried chloride ion.,Altermark B, Smalas AO, Willassen NP, Helland R Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1387-91. Epub 2006, Oct 18. PMID:17057343<ref>PMID:17057343</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2g7e" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The crystal structure of a periplasmic/extracellular endonuclease from Vibrio cholerae has been solved at low and at neutral pH. Crystals grown at pH 4.6 and 6.9 diffracted to 1.6 A (on BM01A at the ESRF) and 1.95 A (on a rotating-anode generator), respectively. The structures of the endonuclease were compared with the structure of a homologous enzyme in V. vulnificus. The structures of the V. cholerae enzyme at different pH values are essentially identical to each other and to the V. vulnificus enzyme. However, interesting features were observed in the solvent structures. Both V. cholerae structures reveal the presence of a chloride ion completely buried within the core of the protein, with the nearest solvent molecule approximately 7 A away. Magnesium, which is essential for catalysis, is present in the structure at neutral pH, but is absent at low pH, and may partly explain the inactivity of the enzyme at lower pH.
*[[Endonuclease 3D structures|Endonuclease 3D structures]]
 
== References ==
==About this Structure==
<references/>
2G7E is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2G7E OCA].
__TOC__
 
</StructureSection>
==Reference==
[[Category: Large Structures]]
The structure of Vibrio cholerae extracellular endonuclease I reveals the presence of a buried chloride ion., Altermark B, Smalas AO, Willassen NP, Helland R, Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1387-91. Epub 2006, Oct 18. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17057343 17057343]
[[Category: Deoxyribonuclease I]]
[[Category: Single protein]]
[[Category: Vibrio cholerae]]
[[Category: Vibrio cholerae]]
[[Category: Altermark, B.]]
[[Category: Altermark B]]
[[Category: Helland, R.]]
[[Category: Helland R]]
[[Category: Smalaas, A O.]]
[[Category: Smalaas AO]]
[[Category: Willassen, N P.]]
[[Category: Willassen NP]]
[[Category: enda]]
[[Category: endonuclease i;buried chloride]]
[[Category: vibrio cholerae nuclease]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:12:49 2008''

Latest revision as of 11:02, 30 October 2024

The 1.6 A crystal structure of Vibrio cholerae extracellular endonuclease IThe 1.6 A crystal structure of Vibrio cholerae extracellular endonuclease I

Structural highlights

2g7e is a 1 chain structure with sequence from Vibrio cholerae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q2XSK9_VIBCL

Evolutionary Conservation

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

Publication Abstract from PubMed

The crystal structure of a periplasmic/extracellular endonuclease from Vibrio cholerae has been solved at low and at neutral pH. Crystals grown at pH 4.6 and 6.9 diffracted to 1.6 A (on BM01A at the ESRF) and 1.95 A (on a rotating-anode generator), respectively. The structures of the endonuclease were compared with the structure of a homologous enzyme in V. vulnificus. The structures of the V. cholerae enzyme at different pH values are essentially identical to each other and to the V. vulnificus enzyme. However, interesting features were observed in the solvent structures. Both V. cholerae structures reveal the presence of a chloride ion completely buried within the core of the protein, with the nearest solvent molecule approximately 7 A away. Magnesium, which is essential for catalysis, is present in the structure at neutral pH, but is absent at low pH, and may partly explain the inactivity of the enzyme at lower pH.

The structure of Vibrio cholerae extracellular endonuclease I reveals the presence of a buried chloride ion.,Altermark B, Smalas AO, Willassen NP, Helland R Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1387-91. Epub 2006, Oct 18. PMID:17057343[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Altermark B, Smalas AO, Willassen NP, Helland R. The structure of Vibrio cholerae extracellular endonuclease I reveals the presence of a buried chloride ion. Acta Crystallogr D Biol Crystallogr. 2006 Nov;62(Pt 11):1387-91. Epub 2006, Oct 18. PMID:17057343 doi:10.1107/S0907444906034196

2g7e, resolution 1.60Å

Drag the structure with the mouse to rotate

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