2hk8: Difference between revisions

Revision as of 03:24, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2hk8.png

Template:STRUCTURE 2hk8

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

Template:ABSTRACT PUBMED 17649975

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

Page seeded by OCA on Tue Jul 29 03:24:45 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2hk8.jpg|left|200px]]
+{{Seed}}
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 {{STRUCTURE_2hk8|  PDB=2hk8  |  SCENE=  }}
-'''Crystal structure of shikimate dehydrogenase from aquifex aeolicus at 2.35 angstrom resolution'''
+===Crystal structure of shikimate dehydrogenase from aquifex aeolicus at 2.35 angstrom resolution===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_17649975}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17649975 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17649975}}
 ==About this Structure==
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 [[Category: Shikimate dehydrogenase]]
 [[Category: Shikimate pathway]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 06:23:19 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:24:45 2008''