2d5c
From Proteopedia
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| - | [[Image:2d5c.gif|left|200px]] | + | [[Image:2d5c.gif|left|200px]] |
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| - | '''Crystal Structure of Shikimate 5-Dehydrogenase (AroE) from Thermus Thermophilus HB8 in complex with shikimate''' | + | {{Structure |
| + | |PDB= 2d5c |SIZE=350|CAPTION= <scene name='initialview01'>2d5c</scene>, resolution 1.65Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=SKM:(3R,4S,5R)-3,4,5-TRIHYDROXYCYCLOHEX-1-ENE-1-CARBOXYLIC ACID'>SKM</scene> | ||
| + | |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=274 Thermus thermophilus]) | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure of Shikimate 5-Dehydrogenase (AroE) from Thermus Thermophilus HB8 in complex with shikimate''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2D5C is a [ | + | 2D5C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D5C OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structures of shikimate dehydrogenase AroE from Thermus thermophilus HB8 and its cofactor and substrate complexes: insights into the enzymatic mechanism., Bagautdinov B, Kunishima N, J Mol Biol. 2007 Oct 19;373(2):424-38. Epub 2007 Aug 21. PMID:[http:// | + | Crystal structures of shikimate dehydrogenase AroE from Thermus thermophilus HB8 and its cofactor and substrate complexes: insights into the enzymatic mechanism., Bagautdinov B, Kunishima N, J Mol Biol. 2007 Oct 19;373(2):424-38. Epub 2007 Aug 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17825835 17825835] |
[[Category: Shikimate dehydrogenase]] | [[Category: Shikimate dehydrogenase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: SO4]] | [[Category: SO4]] | ||
[[Category: dimer]] | [[Category: dimer]] | ||
| - | [[Category: national project on protein structural and functional | + | [[Category: national project on protein structural and functional analyse]] |
[[Category: nppsfa]] | [[Category: nppsfa]] | ||
[[Category: oxidoreductase]] | [[Category: oxidoreductase]] | ||
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[[Category: rsgi]] | [[Category: rsgi]] | ||
[[Category: shikimate]] | [[Category: shikimate]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: substrate]] | [[Category: substrate]] | ||
[[Category: x-ray diffraction]] | [[Category: x-ray diffraction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:23:40 2008'' |
Revision as of 14:23, 20 March 2008
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| , resolution 1.65Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | AroE (Thermus thermophilus) | ||||||
| Activity: | Shikimate dehydrogenase, with EC number 1.1.1.25 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Shikimate 5-Dehydrogenase (AroE) from Thermus Thermophilus HB8 in complex with shikimate
Overview
Shikimate dehydrogenase (EC 1.1.1.25) catalyses the fourth step of the shikimate pathway which is required for the synthesis of the aromatic amino acids and other aromatic compounds in bacteria, microbial eukaryotes, and plants. The crystal structures of the shikimate dehydrogenase AroE from Thermus thermophilus HB8 in its ligand-free form, binary complexes with cofactor NADP+ or substrate shikimate, and the ternary complex with both NADP(H) and shikimate were determined by X-ray diffraction method at atomic resolutions. The crystals are nearly isomorphous with the asymmetric unit containing a dimer, each subunit of which has a bi-domain structure of compact alpha/beta sandwich folds. The two subunits of the enzyme display asymmetry in the crystals due to different relative orientations between the N- and C-terminal domains resulting in a slightly different closure of the interdomain clefts. NADP(H) is bound to the more closed form only. This closed conformation with apparent higher affinity to the cofactor is also observed in the unliganded crystal form, indicating that the NADP(H) binding to TtAroE may follow the selection mode where the cofactor binds to the subunit that happens to be in the closed conformation in solution. Crystal structures of the closed subunits with and without NADP(H) show no significant structural difference, suggesting that the cofactor binding to the closed subunit corresponds to the lock-and-key model in TtAroE. On the other hand, shikimate binds to both open and closed subunit conformers of both apo and NADP(H)-liganded holo enzyme forms. The ternary complex TtAroE:NADP(H):shikimate allows unambiguous visualization of the SDH permitting elucidation of the roles of conserved residues Lys64 and Asp100 in the hydride ion transfer between NADP(H) and shikimate.
About this Structure
2D5C is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Crystal structures of shikimate dehydrogenase AroE from Thermus thermophilus HB8 and its cofactor and substrate complexes: insights into the enzymatic mechanism., Bagautdinov B, Kunishima N, J Mol Biol. 2007 Oct 19;373(2):424-38. Epub 2007 Aug 21. PMID:17825835
Page seeded by OCA on Thu Mar 20 16:23:40 2008
Categories: Shikimate dehydrogenase | Single protein | Thermus thermophilus | Bagautdinov, B. | Kunishima, N. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | SKM | SO4 | Dimer | National project on protein structural and functional analyse | Nppsfa | Oxidoreductase | Riken structural genomics/proteomics initiative | Rsgi | Shikimate | Structural genomic | Substrate | X-ray diffraction
