1nks
From Proteopedia
(New page: 200px<br /><applet load="1nks" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nks, resolution 2.57Å" /> '''ADENYLATE KINASE FRO...) |
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| - | [[Image:1nks.gif|left|200px]]<br /><applet load="1nks" size=" | + | [[Image:1nks.gif|left|200px]]<br /><applet load="1nks" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1nks, resolution 2.57Å" /> | caption="1nks, resolution 2.57Å" /> | ||
'''ADENYLATE KINASE FROM SULFOLOBUS ACIDOCALDARIUS'''<br /> | '''ADENYLATE KINASE FROM SULFOLOBUS ACIDOCALDARIUS'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The adenylate kinase from the hyperthermophilic archaean species | + | The adenylate kinase from the hyperthermophilic archaean species Sulfolobus acidocaldarius has been cloned, expressed in Escherichia coli, purified and crystallized. The crystal structure was elucidated by multiple isomorphous replacement and non-crystallographic density averaging. The structure was refined at 2.6 A (1 A=0.1 nm) resolution. The enzyme is trimeric, in contrast to previous solution measurements that suggested a dimeric structure, and in contrast to the vast majority of adenylate kinases, which are monomeric. In large parts of each subunit the chain fold resembles the known enzyme structure from eubacteria and eukaryotes although the sequence homology is negligible. Since the asymmetric unit contains two trimers with and without bound AMP at the AMP sites and with an ADP at one of the six ATP sites, the analysis shows the enzyme in several states. The conformational differences between these states resemble those of other adenylate kinases. Because of sequence homology, the structure presented provides a good model for the methanococcal adenylate kinases. |
==About this Structure== | ==About this Structure== | ||
| - | 1NKS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius] with AMP and ADP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] Full crystallographic information is available from [http:// | + | 1NKS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_acidocaldarius Sulfolobus acidocaldarius] with <scene name='pdbligand=AMP:'>AMP</scene> and <scene name='pdbligand=ADP:'>ADP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Adenylate_kinase Adenylate kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.3 2.7.4.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NKS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sulfolobus acidocaldarius]] | [[Category: Sulfolobus acidocaldarius]] | ||
| - | [[Category: Schulz, G | + | [[Category: Schulz, G E.]] |
[[Category: Vonrhein, C.]] | [[Category: Vonrhein, C.]] | ||
[[Category: ADP]] | [[Category: ADP]] | ||
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[[Category: transferase]] | [[Category: transferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:12 2008'' |
Revision as of 12:07, 21 February 2008
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ADENYLATE KINASE FROM SULFOLOBUS ACIDOCALDARIUS
Overview
The adenylate kinase from the hyperthermophilic archaean species Sulfolobus acidocaldarius has been cloned, expressed in Escherichia coli, purified and crystallized. The crystal structure was elucidated by multiple isomorphous replacement and non-crystallographic density averaging. The structure was refined at 2.6 A (1 A=0.1 nm) resolution. The enzyme is trimeric, in contrast to previous solution measurements that suggested a dimeric structure, and in contrast to the vast majority of adenylate kinases, which are monomeric. In large parts of each subunit the chain fold resembles the known enzyme structure from eubacteria and eukaryotes although the sequence homology is negligible. Since the asymmetric unit contains two trimers with and without bound AMP at the AMP sites and with an ADP at one of the six ATP sites, the analysis shows the enzyme in several states. The conformational differences between these states resemble those of other adenylate kinases. Because of sequence homology, the structure presented provides a good model for the methanococcal adenylate kinases.
About this Structure
1NKS is a Single protein structure of sequence from Sulfolobus acidocaldarius with and as ligands. Active as Adenylate kinase, with EC number 2.7.4.3 Full crystallographic information is available from OCA.
Reference
The structure of a trimeric archaeal adenylate kinase., Vonrhein C, Bonisch H, Schafer G, Schulz GE, J Mol Biol. 1998 Sep 11;282(1):167-79. PMID:9733648
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