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| {{STRUCTURE_2qes| PDB=2qes | SCENE= }} | | {{STRUCTURE_2qes| PDB=2qes | SCENE= }} |
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| '''Crystal structure of the ribosome inactivating protein PDL4 from P. dioica leaves in complex with adenine'''
| | ===Crystal structure of the ribosome inactivating protein PDL4 from P. dioica leaves in complex with adenine=== |
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| ==Overview==
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| The ribosome inactivating protein PD-L4 from Phytolacca dioica is a N-beta-glycosidase, probably involved in plant defence. The crystal structures of wild type PD-L4 and of the S211A PD-L4 mutant with significantly decreased catalytic activity were determined at atomic resolution. To determine the structural determinants for the reduced activity of S211A PD-L4, both forms have also been co-crystallized with adenine, the major product of PD-L4 catalytic reaction. In the structure of the S211A mutant, the cavity formed by the lack of the Ser hydroxyl group is filled by a water molecule; the insertion of this non-isosteric group leads to small albeit concerted changes in the tightly packed active site of the enzyme. These changes have been correlated to the different activity of the mutant enzyme. This work highlights the importance of atomic resolution studies for the deep understanding of enzymatic properties. Proteins 2008. (c) 2007 Wiley-Liss, Inc.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17963235}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17963235 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17963235}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Hydrolase]] | | [[Category: Hydrolase]] |
| [[Category: Ribosome inactivating protein]] | | [[Category: Ribosome inactivating protein]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:49:51 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:47:16 2008'' |