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1qez

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[[Image:1qez.jpg|left|200px]]<br /><applet load="1qez" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1qez.jpg|left|200px]]
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caption="1qez, resolution 2.70&Aring;" />
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'''SULFOLOBUS ACIDOCALDARIUS INORGANIC PYROPHOSPHATASE: AN ARCHAEL PYROPHOSPHATASE.'''<br />
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{{Structure
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|PDB= 1qez |SIZE=350|CAPTION= <scene name='initialview01'>1qez</scene>, resolution 2.70&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1]
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|GENE=
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}}
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'''SULFOLOBUS ACIDOCALDARIUS INORGANIC PYROPHOSPHATASE: AN ARCHAEL PYROPHOSPHATASE.'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1QEZ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Inorganic_diphosphatase Inorganic diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.1 3.6.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QEZ OCA].
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1QEZ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QEZ OCA].
==Reference==
==Reference==
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Sulfolobus acidocaldarius inorganic pyrophosphatase: structure, thermostability, and effect of metal ion in an archael pyrophosphatase., Leppanen VM, Nummelin H, Hansen T, Lahti R, Schafer G, Goldman A, Protein Sci. 1999 Jun;8(6):1218-31. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10386872 10386872]
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Sulfolobus acidocaldarius inorganic pyrophosphatase: structure, thermostability, and effect of metal ion in an archael pyrophosphatase., Leppanen VM, Nummelin H, Hansen T, Lahti R, Schafer G, Goldman A, Protein Sci. 1999 Jun;8(6):1218-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10386872 10386872]
[[Category: Inorganic diphosphatase]]
[[Category: Inorganic diphosphatase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: thermostability]]
[[Category: thermostability]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:38:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:36:30 2008''

Revision as of 11:36, 20 March 2008


PDB ID 1qez

Drag the structure with the mouse to rotate
, resolution 2.70Å
Ligands:
Activity: Inorganic diphosphatase, with EC number 3.6.1.1
Coordinates: save as pdb, mmCIF, xml



SULFOLOBUS ACIDOCALDARIUS INORGANIC PYROPHOSPHATASE: AN ARCHAEL PYROPHOSPHATASE.


Overview

The first crystal structure of an inorganic pyrophosphatase (S-PPase) from an archaebacterium, the thermophile Sulfolobus acidocaldarius, has been solved by molecular replacement and refined to an R-factor of 19.7% at 2.7 A. S-PPase is a D3 homohexameric protein with one Mg2+ per active site in a position similar to, but not identical with, the first activating metal in mesophilic pyrophosphatases (PPase). In mesophilic PPases, Asp65, Asp70, and Asp102 coordinate the Mg2+, while only Asp65 and Asp102 do in S-PPase, and the Mg2+ moves by 0.7 A. S-PPase may therefore be deactivated at low temperature by mispositioning a key metal ion. The monomer S-PPase structure is very similar to that of Thermus thermophilus (T-PPase) and Escherichia coli (E-PPase), root-mean-square deviations around 1 A/Calpha. But the hexamer structures of S- and T-PPase are more tightly packed and more similar to each other than they are to that of E-PPase, as shown by the increase in surface area buried upon oligomerization. In T-PPase, Arg116 creates an interlocking ionic network to both twofold and threefold related monomers; S-PPase has hydrophilic interactions to threefold related monomers absent in both E- and T-PPase. In addition, the thermostable PPases have about 7% more hydrogen bonds per monomer than E-PPase, and, especially in S-PPase, additional ionic interactions anchor the C-terminus to the rest of the protein. Thermostability in PPases is thus due to subtle improvements in both monomer and oligomer interactions.

About this Structure

1QEZ is a Single protein structure of sequence from Sulfolobus acidocaldarius. Full crystallographic information is available from OCA.

Reference

Sulfolobus acidocaldarius inorganic pyrophosphatase: structure, thermostability, and effect of metal ion in an archael pyrophosphatase., Leppanen VM, Nummelin H, Hansen T, Lahti R, Schafer G, Goldman A, Protein Sci. 1999 Jun;8(6):1218-31. PMID:10386872

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