2az1

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(New page: 200px<br /><applet load="2az1" size="450" color="white" frame="true" align="right" spinBox="true" caption="2az1, resolution 2.35&Aring;" /> '''Structure of a halop...)
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[[Image:2az1.gif|left|200px]]<br /><applet load="2az1" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2az1, resolution 2.35&Aring;" />
caption="2az1, resolution 2.35&Aring;" />
'''Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum'''<br />
'''Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum'''<br />
==Overview==
==Overview==
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Nucleoside diphosphate kinase from the halophilic archaeon Halobacterium, salinarum was crystallized in a free state and a substrate-bound form with, CDP. The structures were solved to a resolution of 2.35 and 2.2A, respectively. Crystals with the apo-form were obtained with His6-tagged, enzyme, whereas the untagged form was used for co-crystallization with the, nucleotide. Crosslinking under different salt and pH conditions revealed a, stronger oligomerization tendency for the tagged protein at low and high, salt concentrations. The influence of the His6-tag on the halophilic, nature of the enzyme is discussed on the basis of the observed structural, properties.
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Nucleoside diphosphate kinase from the halophilic archaeon Halobacterium salinarum was crystallized in a free state and a substrate-bound form with CDP. The structures were solved to a resolution of 2.35 and 2.2A, respectively. Crystals with the apo-form were obtained with His6-tagged enzyme, whereas the untagged form was used for co-crystallization with the nucleotide. Crosslinking under different salt and pH conditions revealed a stronger oligomerization tendency for the tagged protein at low and high salt concentrations. The influence of the His6-tag on the halophilic nature of the enzyme is discussed on the basis of the observed structural properties.
==About this Structure==
==About this Structure==
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2AZ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2AZ1 OCA].
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2AZ1 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Nucleoside-diphosphate_kinase Nucleoside-diphosphate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.6 2.7.4.6] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AZ1 OCA].
==Reference==
==Reference==
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[[Category: surface charges]]
[[Category: surface charges]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:28:30 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:29 2008''

Revision as of 14:32, 21 February 2008


2az1, resolution 2.35Å

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Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum

Overview

Nucleoside diphosphate kinase from the halophilic archaeon Halobacterium salinarum was crystallized in a free state and a substrate-bound form with CDP. The structures were solved to a resolution of 2.35 and 2.2A, respectively. Crystals with the apo-form were obtained with His6-tagged enzyme, whereas the untagged form was used for co-crystallization with the nucleotide. Crosslinking under different salt and pH conditions revealed a stronger oligomerization tendency for the tagged protein at low and high salt concentrations. The influence of the His6-tag on the halophilic nature of the enzyme is discussed on the basis of the observed structural properties.

About this Structure

2AZ1 is a Single protein structure of sequence from Halobacterium salinarum with as ligand. Active as Nucleoside-diphosphate kinase, with EC number 2.7.4.6 Full crystallographic information is available from OCA.

Reference

Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum., Besir H, Zeth K, Bracher A, Heider U, Ishibashi M, Tokunaga M, Oesterhelt D, FEBS Lett. 2005 Dec 5;579(29):6595-600. Epub 2005 Nov 9. PMID:16293253

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