1obw

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1obw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1obw, resolution 1.9&Aring;" /> '''STRUCTURE OF INORGANI...)
Line 1: Line 1:
-
[[Image:1obw.jpg|left|200px]]<br /><applet load="1obw" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1obw.jpg|left|200px]]<br /><applet load="1obw" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1obw, resolution 1.9&Aring;" />
caption="1obw, resolution 1.9&Aring;" />
'''STRUCTURE OF INORGANIC PYROPHOSPHATASE'''<br />
'''STRUCTURE OF INORGANIC PYROPHOSPHATASE'''<br />
==Overview==
==Overview==
-
Crystalline holo inorganic pyrophosphatase from Escherichia coli was grown, in the presence of 250 mM MgCl2. The crystal structure has been solved by, Patterson search techniques and refined to an R-factor of 17.6% at 1.9 A, resolution. The upper estimate of the root-mean-square error in atomic, positions is 0.26 A. These crystals belong to space group P3(2)21 with, unit cell dimensions a = b = 110.27 A and c = 78.17 A. The asymmetric unit, contains a trimer of subunits, i.e., half of the hexameric molecule. In, the central cavity of the enzyme molecule, three Mg2+ ions, each shared by, two subunits of the hexamer, are found. In the active sites of two, crystallographically independent subunits, two Mg2+ ions are bound. The, second active site Mg2+ ion is missing in the third subunit. A mechanism, of catalysis is proposed whereby a water molecule activated by a Mg2+ ion, and Tyr 55 play essential roles.
+
Crystalline holo inorganic pyrophosphatase from Escherichia coli was grown in the presence of 250 mM MgCl2. The crystal structure has been solved by Patterson search techniques and refined to an R-factor of 17.6% at 1.9 A resolution. The upper estimate of the root-mean-square error in atomic positions is 0.26 A. These crystals belong to space group P3(2)21 with unit cell dimensions a = b = 110.27 A and c = 78.17 A. The asymmetric unit contains a trimer of subunits, i.e., half of the hexameric molecule. In the central cavity of the enzyme molecule, three Mg2+ ions, each shared by two subunits of the hexamer, are found. In the active sites of two crystallographically independent subunits, two Mg2+ ions are bound. The second active site Mg2+ ion is missing in the third subunit. A mechanism of catalysis is proposed whereby a water molecule activated by a Mg2+ ion and Tyr 55 play essential roles.
==About this Structure==
==About this Structure==
-
1OBW 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 MG 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OBW OCA].
+
1OBW 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> 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=1OBW OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Inorganic diphosphatase]]
[[Category: Inorganic diphosphatase]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Avaeva, S.M.]]
+
[[Category: Avaeva, S M.]]
-
[[Category: Harutyunyan, E.H.]]
+
[[Category: Harutyunyan, E H.]]
[[Category: Huber, R.]]
[[Category: Huber, R.]]
[[Category: Mather, T.]]
[[Category: Mather, T.]]
-
[[Category: Oganessyan, N.N.]]
+
[[Category: Oganessyan, N N.]]
-
[[Category: Oganessyan, V.Yu.]]
+
[[Category: Oganessyan, V Yu.]]
[[Category: MG]]
[[Category: MG]]
[[Category: 3d-structure]]
[[Category: 3d-structure]]
Line 26: Line 26:
[[Category: metal binding]]
[[Category: metal binding]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:54:20 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:54 2008''

Revision as of 12:15, 21 February 2008


1obw, resolution 1.9Å

Drag the structure with the mouse to rotate

STRUCTURE OF INORGANIC PYROPHOSPHATASE

Overview

Crystalline holo inorganic pyrophosphatase from Escherichia coli was grown in the presence of 250 mM MgCl2. The crystal structure has been solved by Patterson search techniques and refined to an R-factor of 17.6% at 1.9 A resolution. The upper estimate of the root-mean-square error in atomic positions is 0.26 A. These crystals belong to space group P3(2)21 with unit cell dimensions a = b = 110.27 A and c = 78.17 A. The asymmetric unit contains a trimer of subunits, i.e., half of the hexameric molecule. In the central cavity of the enzyme molecule, three Mg2+ ions, each shared by two subunits of the hexamer, are found. In the active sites of two crystallographically independent subunits, two Mg2+ ions are bound. The second active site Mg2+ ion is missing in the third subunit. A mechanism of catalysis is proposed whereby a water molecule activated by a Mg2+ ion and Tyr 55 play essential roles.

About this Structure

1OBW is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Inorganic diphosphatase, with EC number 3.6.1.1 Full crystallographic information is available from OCA.

Reference

Crystal structure of holo inorganic pyrophosphatase from Escherichia coli at 1.9 A resolution. Mechanism of hydrolysis., Harutyunyan EH, Oganessyan VY, Oganessyan NN, Avaeva SM, Nazarova TI, Vorobyeva NN, Kurilova SA, Huber R, Mather T, Biochemistry. 1997 Jun 24;36(25):7754-60. PMID:9201917

Page seeded by OCA on Thu Feb 21 14:15:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools