2d3b: Difference between revisions

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New page: left|200px<br /><applet load="2d3b" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d3b, resolution 3.50Å" /> '''Crystal Structure of...
 
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caption="2d3b, resolution 3.50&Aring;" />
caption="2d3b, resolution 3.50&Aring;" />
'''Crystal Structure of the Maize Glutamine Synthetase complexed with AMPPNP and Methionine sulfoximine'''<br />
'''Crystal Structure of the Maize Glutamine Synthetase complexed with AMPPNP and Methionine sulfoximine'''<br />


==Overview==
==Overview==
Plants provide nourishment for animals and other heterotrophs as the sole, primary producer in the food chain. Glutamine synthetase (GS), one of the, essential enzymes for plant autotrophy catalyzes the incorporation of, ammonia into glutamate to generate glutamine with concomitant hydrolysis, of ATP, and plays a crucial role in the assimilation and re-assimilation, of ammonia derived from a wide variety of metabolic processes during plant, growth and development. Elucidation of the atomic structure of higher, plant GS is important to understand its detailed reaction mechanism and to, obtain further insight into plant productivity and agronomical utility., Here we report the first crystal structures of maize (Zea mays L.) GS. The, structure reveals a unique decameric structure that differs significantly, from the bacterial GS structure. Higher plants have several isoenzymes of, GS differing in heat stability and catalytic properties for efficient, responses to variation in the environment and nutrition. A key residue, responsible for the heat stability was found to be Ile-161 in GS1a. The, three structures in complex with substrate analogues, including, phosphinothricin, a widely used herbicide, lead us to propose a mechanism, for the transfer of phosphate from ATP to glutamate and to interpret the, inhibitory action of phosphinothricin as a guide for the development of, new potential herbicides.
Plants provide nourishment for animals and other heterotrophs as the sole primary producer in the food chain. Glutamine synthetase (GS), one of the essential enzymes for plant autotrophy catalyzes the incorporation of ammonia into glutamate to generate glutamine with concomitant hydrolysis of ATP, and plays a crucial role in the assimilation and re-assimilation of ammonia derived from a wide variety of metabolic processes during plant growth and development. Elucidation of the atomic structure of higher plant GS is important to understand its detailed reaction mechanism and to obtain further insight into plant productivity and agronomical utility. Here we report the first crystal structures of maize (Zea mays L.) GS. The structure reveals a unique decameric structure that differs significantly from the bacterial GS structure. Higher plants have several isoenzymes of GS differing in heat stability and catalytic properties for efficient responses to variation in the environment and nutrition. A key residue responsible for the heat stability was found to be Ile-161 in GS1a. The three structures in complex with substrate analogues, including phosphinothricin, a widely used herbicide, lead us to propose a mechanism for the transfer of phosphate from ATP to glutamate and to interpret the inhibitory action of phosphinothricin as a guide for the development of new potential herbicides.


==About this Structure==
==About this Structure==
2D3B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with MN, MSL and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.2 6.3.1.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D3B OCA].  
2D3B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=MSL:'>MSL</scene> and <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Glutamate--ammonia_ligase Glutamate--ammonia ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.1.2 6.3.1.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D3B OCA].  


==Reference==
==Reference==
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[[Category: glutamine synthetase maize]]
[[Category: glutamine synthetase maize]]


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Revision as of 17:55, 21 February 2008

File:2d3b.gif


2d3b, resolution 3.50Å

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Crystal Structure of the Maize Glutamine Synthetase complexed with AMPPNP and Methionine sulfoximine

OverviewOverview

Plants provide nourishment for animals and other heterotrophs as the sole primary producer in the food chain. Glutamine synthetase (GS), one of the essential enzymes for plant autotrophy catalyzes the incorporation of ammonia into glutamate to generate glutamine with concomitant hydrolysis of ATP, and plays a crucial role in the assimilation and re-assimilation of ammonia derived from a wide variety of metabolic processes during plant growth and development. Elucidation of the atomic structure of higher plant GS is important to understand its detailed reaction mechanism and to obtain further insight into plant productivity and agronomical utility. Here we report the first crystal structures of maize (Zea mays L.) GS. The structure reveals a unique decameric structure that differs significantly from the bacterial GS structure. Higher plants have several isoenzymes of GS differing in heat stability and catalytic properties for efficient responses to variation in the environment and nutrition. A key residue responsible for the heat stability was found to be Ile-161 in GS1a. The three structures in complex with substrate analogues, including phosphinothricin, a widely used herbicide, lead us to propose a mechanism for the transfer of phosphate from ATP to glutamate and to interpret the inhibitory action of phosphinothricin as a guide for the development of new potential herbicides.

About this StructureAbout this Structure

2D3B is a Single protein structure of sequence from Zea mays with , and as ligands. Active as Glutamate--ammonia ligase, with EC number 6.3.1.2 Full crystallographic information is available from OCA.

ReferenceReference

Atomic structure of plant glutamine synthetase: a key enzyme for plant productivity., Unno H, Uchida T, Sugawara H, Kurisu G, Sugiyama T, Yamaya T, Sakakibara H, Hase T, Kusunoki M, J Biol Chem. 2006 Sep 29;281(39):29287-96. Epub 2006 Jul 7. PMID:16829528

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