2hk8: Difference between revisions

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[[Image:2hk8.jpg|left|200px]]<br /><applet load="2hk8" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2hk8.jpg|left|200px]]
caption="2hk8, resolution 2.35&Aring;" />
 
'''Crystal structure of shikimate dehydrogenase from aquifex aeolicus at 2.35 angstrom resolution'''<br />
{{Structure
|PDB= 2hk8 |SIZE=350|CAPTION= <scene name='initialview01'>2hk8</scene>, resolution 2.35&Aring;
|SITE=
|LIGAND=
|ACTIVITY= [http://en.wikipedia.org/wiki/Shikimate_dehydrogenase Shikimate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.25 1.1.1.25]
|GENE= aroE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=63363 Aquifex aeolicus])
}}
 
'''Crystal structure of shikimate dehydrogenase from aquifex aeolicus at 2.35 angstrom resolution'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2HK8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Active as [http://en.wikipedia.org/wiki/Shikimate_dehydrogenase Shikimate dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.25 1.1.1.25] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HK8 OCA].  
2HK8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Aquifex_aeolicus Aquifex aeolicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HK8 OCA].  


==Reference==
==Reference==
Structural and biochemical analyses of shikimate dehydrogenase AroE from Aquifex aeolicus: implications for the catalytic mechanism., Gan J, Wu Y, Prabakaran P, Gu Y, Li Y, Andrykovitch M, Liu H, Gong Y, Yan H, Ji X, Biochemistry. 2007 Aug 21;46(33):9513-22. Epub 2007 Jul 25. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17649975 17649975]
Structural and biochemical analyses of shikimate dehydrogenase AroE from Aquifex aeolicus: implications for the catalytic mechanism., Gan J, Wu Y, Prabakaran P, Gu Y, Li Y, Andrykovitch M, Liu H, Gong Y, Yan H, Ji X, Biochemistry. 2007 Aug 21;46(33):9513-22. Epub 2007 Jul 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17649975 17649975]
[[Category: Aquifex aeolicus]]
[[Category: Aquifex aeolicus]]
[[Category: Shikimate dehydrogenase]]
[[Category: Shikimate dehydrogenase]]
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[[Category: shikimate pathway]]
[[Category: shikimate pathway]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:42:43 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:18:13 2008''

Revision as of 18:18, 20 March 2008

File:2hk8.jpg


PDB ID 2hk8

Drag the structure with the mouse to rotate
, resolution 2.35Å
Gene: aroE (Aquifex aeolicus)
Activity: Shikimate dehydrogenase, with EC number 1.1.1.25
Coordinates: save as pdb, mmCIF, xml



Crystal structure of shikimate dehydrogenase from aquifex aeolicus at 2.35 angstrom resolution


OverviewOverview

The shikimate biosynthetic pathway is essential to microorganisms, plants, and parasites but absent from mammals. Therefore, shikimate dehydrogenase (SD) and other enzymes in the pathway are attractive targets for developing nontoxic antimicrobial agents, herbicides, and antiparasite drugs. SD catalyzes the fourth reaction in the pathway, the nicotinamide adenine dinucleotide phosphate- (NADP-) dependent reduction of 3-dehydroshikimic acid to shikimic acid (SA), as well as its reverse, by the transfer of a hydride. Previous structural studies reveal that the enzyme exists in two major conformations, an open and a closed form. For the reaction to occur, it is believed that the catalytic complex assumes the closed conformation. Nonetheless, the only structure containing both SA and NADP+ exhibits an open conformation (PDB entry 2EV9). Here, we present two crystal structures of Aquifex aeolicus SD, including a ternary complex with both SA and NADP+, which assumes the closed conformation and therefore contains a catalytically competent active site. On the basis of preexisting and novel structural and biochemical data, a catalytic mechanism is proposed.

About this StructureAbout this Structure

2HK8 is a Single protein structure of sequence from Aquifex aeolicus. Full crystallographic information is available from OCA.

ReferenceReference

Structural and biochemical analyses of shikimate dehydrogenase AroE from Aquifex aeolicus: implications for the catalytic mechanism., Gan J, Wu Y, Prabakaran P, Gu Y, Li Y, Andrykovitch M, Liu H, Gong Y, Yan H, Ji X, Biochemistry. 2007 Aug 21;46(33):9513-22. Epub 2007 Jul 25. PMID:17649975

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