1igp
From Proteopedia
(New page: 200px<br /><applet load="1igp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1igp, resolution 2.2Å" /> '''X-RAY CRYSTALLOGRAPHI...) |
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| - | [[Image:1igp.gif|left|200px]]<br /><applet load="1igp" size=" | + | [[Image:1igp.gif|left|200px]]<br /><applet load="1igp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1igp, resolution 2.2Å" /> | caption="1igp, resolution 2.2Å" /> | ||
'''X-RAY CRYSTALLOGRAPHIC STUDIES OF RECOMBINANT INORGANIC PYROPHOSPHATASE FROM ESCHERICHIA COLI'''<br /> | '''X-RAY CRYSTALLOGRAPHIC STUDIES OF RECOMBINANT INORGANIC PYROPHOSPHATASE FROM ESCHERICHIA COLI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | An E. coli inorganic pyrophosphatase overproducer and a method for a | + | An E. coli inorganic pyrophosphatase overproducer and a method for a large-scale production of the homogeneous enzyme are described. The inorganic pyrophosphatase was crystallized in the form containing one subunit of a homohexameric molecule per asymmetric unit: space group R32, a = 110.4 A, c = 76.8 A. The electron density map to 2.5 A resolution phased with Eu- and Hg-derivatives (figure of merit, <m> = 0.51) was improved by the solvent flattening procedure (<m> = 0.77). The course of the polypeptide chain and the secondary structure elements, intersubunit contacts and positions of the active sites were characterized. Homology with S. cerevisiae inorganic pyrophosphatase structure was found. |
==About this Structure== | ==About this Structure== | ||
| - | 1IGP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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:// | + | 1IGP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. 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=1IGP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Inorganic diphosphatase]] | [[Category: Inorganic diphosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Avaeva, S | + | [[Category: Avaeva, S M.]] |
| - | [[Category: Harutyunyan, E | + | [[Category: Harutyunyan, E H.]] |
| - | [[Category: Oganessyan, V | + | [[Category: Oganessyan, V Yu.]] |
[[Category: acid anhydride hydrolase]] | [[Category: acid anhydride hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:11:42 2008'' |
Revision as of 11:11, 21 February 2008
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X-RAY CRYSTALLOGRAPHIC STUDIES OF RECOMBINANT INORGANIC PYROPHOSPHATASE FROM ESCHERICHIA COLI
Overview
An E. coli inorganic pyrophosphatase overproducer and a method for a large-scale production of the homogeneous enzyme are described. The inorganic pyrophosphatase was crystallized in the form containing one subunit of a homohexameric molecule per asymmetric unit: space group R32, a = 110.4 A, c = 76.8 A. The electron density map to 2.5 A resolution phased with Eu- and Hg-derivatives (figure of merit, <m> = 0.51) was improved by the solvent flattening procedure (<m> = 0.77). The course of the polypeptide chain and the secondary structure elements, intersubunit contacts and positions of the active sites were characterized. Homology with S. cerevisiae inorganic pyrophosphatase structure was found.
About this Structure
1IGP is a Single protein structure of sequence from Escherichia coli. Active as Inorganic diphosphatase, with EC number 3.6.1.1 Full crystallographic information is available from OCA.
Reference
X-ray crystallographic studies of recombinant inorganic pyrophosphatase from Escherichia coli., Oganessyan VYu, Kurilova SA, Vorobyeva NN, Nazarova TI, Popov AN, Lebedev AA, Avaeva SM, Harutyunyan EH, FEBS Lett. 1994 Jul 18;348(3):301-4. PMID:8034059
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