2bd0
From Proteopedia
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| - | [[Image:2bd0.gif|left|200px]] | + | [[Image:2bd0.gif|left|200px]] |
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| - | '''Chlorobium tepidum Sepiapterin Reductase complexed with NADP and Sepiapterin''' | + | {{Structure |
| + | |PDB= 2bd0 |SIZE=350|CAPTION= <scene name='initialview01'>2bd0</scene>, resolution 1.700Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene> and <scene name='pdbligand=BIO:BIOPTERIN'>BIO</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Sepiapterin_reductase Sepiapterin reductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.153 1.1.1.153] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Chlorobium tepidum Sepiapterin Reductase complexed with NADP and Sepiapterin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BD0 is a [ | + | 2BD0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Chlorobaculum_tepidum Chlorobaculum tepidum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BD0 OCA]. |
==Reference== | ==Reference== | ||
| - | Structure of Chlorobium tepidum sepiapterin reductase complex reveals the novel substrate binding mode for stereospecific production of L-threo-tetrahydrobiopterin., Supangat S, Seo KH, Choi YK, Park YS, Son D, Han CD, Lee KH, J Biol Chem. 2006 Jan 27;281(4):2249-56. Epub 2005 Nov 24. PMID:[http:// | + | Structure of Chlorobium tepidum sepiapterin reductase complex reveals the novel substrate binding mode for stereospecific production of L-threo-tetrahydrobiopterin., Supangat S, Seo KH, Choi YK, Park YS, Son D, Han CD, Lee KH, J Biol Chem. 2006 Jan 27;281(4):2249-56. Epub 2005 Nov 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16308317 16308317] |
[[Category: Chlorobaculum tepidum]] | [[Category: Chlorobaculum tepidum]] | ||
[[Category: Sepiapterin reductase]] | [[Category: Sepiapterin reductase]] | ||
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[[Category: sepiapterin reductase]] | [[Category: sepiapterin reductase]] | ||
| - | ''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 16:00:19 2008'' |
Revision as of 14:00, 20 March 2008
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| , resolution 1.700Å | |||||||
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| Ligands: | and | ||||||
| Activity: | Sepiapterin reductase, with EC number 1.1.1.153 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Chlorobium tepidum Sepiapterin Reductase complexed with NADP and Sepiapterin
Overview
Sepiapterin reductase (SR) is involved in the last step of tetrahydrobiopterin (BH(4)) biosynthesis by reducing the di-keto group of 6-pyruvoyl tetrahydropterin. Chlorobium tepidum SR (cSR) generates a distinct BH(4) product, L-threo-BH(4) (6R-(1'S,2'S)-5,6,7,8-BH(4)), whereas animal enzymes produce L-erythro-BH(4) (6R-(1'R,2'S)-5,6,7,8-BH(4)) although it has high amino acid sequence similarities to the other animal enzymes. To elucidate the structural basis for the different reaction stereospecificities, we have determined the three-dimensional structures of cSR alone and complexed with NADP and sepiapterin at 2.1 and 1.7 A resolution, respectively. The overall folding of the cSR, the binding site for the cofactor NADP(H), and the positions of active site residues were quite similar to the mouse and the human SR. However, significant differences were found in the substrate binding region of the cSR. In comparison to the mouse SR complex, the sepiapterin in the cSR is rotated about 180 degrees around the active site and bound between two aromatic side chains of Trp-196 and Phe-99 so that its pterin ring is shifted to the opposite side, but its side chain position is not changed. The swiveled sepiapterin binding results in the conversion of the side chain configuration, exposing the opposite face for hydride transfer from NADPH. The different sepiapterin binding mode within the conserved catalytic architecture presents a novel strategy of switching the reaction stereospecificities in the same protein fold.
About this Structure
2BD0 is a Single protein structure of sequence from Chlorobaculum tepidum. Full crystallographic information is available from OCA.
Reference
Structure of Chlorobium tepidum sepiapterin reductase complex reveals the novel substrate binding mode for stereospecific production of L-threo-tetrahydrobiopterin., Supangat S, Seo KH, Choi YK, Park YS, Son D, Han CD, Lee KH, J Biol Chem. 2006 Jan 27;281(4):2249-56. Epub 2005 Nov 24. PMID:16308317
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