1nns

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(New page: 200px<br /><applet load="1nns" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nns, resolution 1.95&Aring;" /> '''L-asparaginase of E....)
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[[Image:1nns.gif|left|200px]]<br /><applet load="1nns" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nns, resolution 1.95&Aring;" />
caption="1nns, resolution 1.95&Aring;" />
'''L-asparaginase of E. coli in C2 space group and 1.95 A resolution'''<br />
'''L-asparaginase of E. coli in C2 space group and 1.95 A resolution'''<br />
==Overview==
==Overview==
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The functional L-asparaginase from Escherichia coli is a homotetramer with, a molecular weight of about 142 kDa. The X-ray structure of the enzyme, crystallized in a new form (space group C2) and refined to 1.95 A, resolution, is compared with that of the previously determined crystal, form (space group P2(1)). The asymmetric unit of the new crystal form, contains an L-asparaginase dimer instead of the tetramer found in the, previous crystal form. It is found that crystal contacts practically do, not affect the conformation of the protein. It is shown that subunit C of, the tetrameric form is in a conformation which is systematically different, from that of all other subunits in both crystal forms. Major, conformational differences are confined to the lid loop (residues 14-27)., In addition, the stability of this globular protein is analyzed in terms, of the interactions between hydrophobic parts of the subunits.
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The functional L-asparaginase from Escherichia coli is a homotetramer with a molecular weight of about 142 kDa. The X-ray structure of the enzyme, crystallized in a new form (space group C2) and refined to 1.95 A resolution, is compared with that of the previously determined crystal form (space group P2(1)). The asymmetric unit of the new crystal form contains an L-asparaginase dimer instead of the tetramer found in the previous crystal form. It is found that crystal contacts practically do not affect the conformation of the protein. It is shown that subunit C of the tetrameric form is in a conformation which is systematically different from that of all other subunits in both crystal forms. Major conformational differences are confined to the lid loop (residues 14-27). In addition, the stability of this globular protein is analyzed in terms of the interactions between hydrophobic parts of the subunits.
==About this Structure==
==About this Structure==
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1NNS 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 ASP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NNS OCA].
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1NNS 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=ASP:'>ASP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Asparaginase Asparaginase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.1 3.5.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NNS OCA].
==Reference==
==Reference==
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Barbosa, J.A.R.G.]]
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[[Category: Barbosa, J A.R G.]]
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[[Category: Neto, J.A.A.]]
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[[Category: Neto, J A.A.]]
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[[Category: Oliveira, R.T.de.]]
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[[Category: Oliveira, R T.de.]]
[[Category: Polikarpov, I.]]
[[Category: Polikarpov, I.]]
[[Category: Sanches, M.]]
[[Category: Sanches, M.]]
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[[Category: l-asparaginase]]
[[Category: l-asparaginase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:24:56 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:08:06 2008''

Revision as of 12:08, 21 February 2008


1nns, resolution 1.95Å

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L-asparaginase of E. coli in C2 space group and 1.95 A resolution

Overview

The functional L-asparaginase from Escherichia coli is a homotetramer with a molecular weight of about 142 kDa. The X-ray structure of the enzyme, crystallized in a new form (space group C2) and refined to 1.95 A resolution, is compared with that of the previously determined crystal form (space group P2(1)). The asymmetric unit of the new crystal form contains an L-asparaginase dimer instead of the tetramer found in the previous crystal form. It is found that crystal contacts practically do not affect the conformation of the protein. It is shown that subunit C of the tetrameric form is in a conformation which is systematically different from that of all other subunits in both crystal forms. Major conformational differences are confined to the lid loop (residues 14-27). In addition, the stability of this globular protein is analyzed in terms of the interactions between hydrophobic parts of the subunits.

About this Structure

1NNS is a Single protein structure of sequence from Escherichia coli with as ligand. Active as Asparaginase, with EC number 3.5.1.1 Full crystallographic information is available from OCA.

Reference

Structural comparison of Escherichia coli L-asparaginase in two monoclinic space groups., Sanches M, Barbosa JA, de Oliveira RT, Abrahao Neto J, Polikarpov I, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):416-22. Epub 2003, Feb 21. PMID:12595697

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