2az3
From Proteopedia
(New page: 200px<br /><applet load="2az3" size="450" color="white" frame="true" align="right" spinBox="true" caption="2az3, resolution 2.20Å" /> '''Structure of a halop...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:2az3.gif|left|200px]]<br /><applet load="2az3" size=" | + | [[Image:2az3.gif|left|200px]]<br /><applet load="2az3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2az3, resolution 2.20Å" /> | caption="2az3, resolution 2.20Å" /> | ||
'''Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum in complex with CDP'''<br /> | '''Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum in complex with CDP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Nucleoside diphosphate kinase from the halophilic archaeon Halobacterium | + | 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== | ||
| - | 2AZ3 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 MG and CDP as [http://en.wikipedia.org/wiki/ligands ligands]. 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:// | + | 2AZ3 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=MG:'>MG</scene> and <scene name='pdbligand=CDP:'>CDP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=2AZ3 OCA]. |
==Reference== | ==Reference== | ||
| Line 25: | Line 25: | ||
[[Category: halophilic]] | [[Category: halophilic]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:32:35 2008'' |
Revision as of 14:32, 21 February 2008
|
Structure of a halophilic nucleoside diphosphate kinase from Halobacterium salinarum in complex with CDP
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
2AZ3 is a Single protein structure of sequence from Halobacterium salinarum with and as ligands. 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
Page seeded by OCA on Thu Feb 21 16:32:35 2008
