1h46
From Proteopedia
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| - | [[Image:1h46.gif|left|200px]] | + | [[Image:1h46.gif|left|200px]] |
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| - | '''THE CATALYTIC MODULE OF CEL7D FROM PHANEROCHAETE CHRYSOSPORIUM AS A CHIRAL SELECTOR: STRUCTURAL STUDIES OF ITS COMPLEX WITH THE B-BLOCKER (R)-PROPRANOLOL''' | + | {{Structure |
| + | |PDB= 1h46 |SIZE=350|CAPTION= <scene name='initialview01'>1h46</scene>, resolution 1.52Å | ||
| + | |SITE= <scene name='pdbsite=NAG:Catalytic+Residues+Chain+X,+GLU+X+207+Nucleophile+,GLU+X+...'>NAG</scene> | ||
| + | |LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=RNP:(1E,2R)-1-(ISOPROPYLIMINO)-3-(1-NAPHTHYLOXY)PROPAN-2-OL'>RNP</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''THE CATALYTIC MODULE OF CEL7D FROM PHANEROCHAETE CHRYSOSPORIUM AS A CHIRAL SELECTOR: STRUCTURAL STUDIES OF ITS COMPLEX WITH THE B-BLOCKER (R)-PROPRANOLOL''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1H46 is a [ | + | 1H46 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Phanerochaete_chrysosporium Phanerochaete chrysosporium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H46 OCA]. |
==Reference== | ==Reference== | ||
| - | The catalytic module of Cel7D from Phanerochaete chrysosporium as a chiral selector: structural studies of its complex with the beta blocker (R)-propranolol., Munoz IG, Mowbray SL, Stahlberg J, Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):637-43. Epub 2003, Mar 25. PMID:[http:// | + | The catalytic module of Cel7D from Phanerochaete chrysosporium as a chiral selector: structural studies of its complex with the beta blocker (R)-propranolol., Munoz IG, Mowbray SL, Stahlberg J, Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):637-43. Epub 2003, Mar 25. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12657782 12657782] |
[[Category: Cellulose 1,4-beta-cellobiosidase]] | [[Category: Cellulose 1,4-beta-cellobiosidase]] | ||
[[Category: Phanerochaete chrysosporium]] | [[Category: Phanerochaete chrysosporium]] | ||
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[[Category: glycoside hydrolase]] | [[Category: glycoside hydrolase]] | ||
| - | ''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 11:32:01 2008'' |
Revision as of 09:32, 20 March 2008
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| , resolution 1.52Å | |||||||
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| Sites: | |||||||
| Ligands: | and | ||||||
| Activity: | Cellulose 1,4-beta-cellobiosidase, with EC number 3.2.1.91 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CATALYTIC MODULE OF CEL7D FROM PHANEROCHAETE CHRYSOSPORIUM AS A CHIRAL SELECTOR: STRUCTURAL STUDIES OF ITS COMPLEX WITH THE B-BLOCKER (R)-PROPRANOLOL
Overview
Previous investigations have shown that the major cellobiohydrolase of Phanerochaete chrysosporium, Cel7D (CBH 58), can be used to separate the enantiomers of a number of drugs, including adrenergic beta blockers such as propranolol. The structural basis of this enantioselectivity is explored here. A 1.5 A X-ray structure of the catalytic domain of Cel7D in complex with (R)-propranolol showed the ligand bound at the active site in glucosyl-binding subsites -1/+1. The catalytic residue Glu207 makes a strong charge-charge interaction with the secondary amine of (R)-propranolol; this is supported by a second interaction of the amine with the nearby Asp209. The aromatic naphthyl group stacks onto the indole ring of Trp373 (normally the glucosyl-binding platform of subsite +1). Other factors also contribute to good complementarity between the ligand and the substrate-binding cleft of the enzyme. Comparison with the previous structure of a related cellulase, Cel7A from Trichoderma reesei, in complex with (S)-propranolol strongly suggests that these enzymes will bind the (S)-enantiomer in a very similar manner, distinct from their mode of binding to (R)-propranolol. Tighter binding of both enzymes to the (S)-enantiomer is largely explained by two additional hydrogen-bonding interactions with its hydroxyl group. The distinct preference for the (R)-enantiomer is probably a consequence of structural differences near the naphthyl group of the ligand.
About this Structure
1H46 is a Single protein structure of sequence from Phanerochaete chrysosporium. Full crystallographic information is available from OCA.
Reference
The catalytic module of Cel7D from Phanerochaete chrysosporium as a chiral selector: structural studies of its complex with the beta blocker (R)-propranolol., Munoz IG, Mowbray SL, Stahlberg J, Acta Crystallogr D Biol Crystallogr. 2003 Apr;59(Pt 4):637-43. Epub 2003, Mar 25. PMID:12657782
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