2z4u: Difference between revisions

Revision as of 21:36, 28 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:2z4u.png

Template:STRUCTURE 2z4u

Crystal structure of wild type PD-L4 from Phytolacca dioica leavesCrystal structure of wild type PD-L4 from Phytolacca dioica leaves

Template:ABSTRACT PUBMED 17963235

About this StructureAbout this Structure

2Z4U is a Single protein structure of sequence from Phytolacca dioica. Full crystallographic information is available from OCA.

ReferenceReference

Atomic resolution (1.1 A) structure of the ribosome-inactivating protein PD-L4 from Phytolacca dioica L. leaves., Ruggiero A, Chambery A, Maro AD, Parente A, Berisio R, Proteins. 2007 Oct 26;71(1):8-15. PMID:17963235

Page seeded by OCA on Mon Jul 28 21:36:22 2008

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

OCA

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-'''Crystal structure of wild type PD-L4 from Phytolacca dioica leaves'''
+===Crystal structure of wild type PD-L4 from Phytolacca dioica leaves===
-==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
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 [[Category: Ribosome-inactivating protein]]
 [[Category: X-ray]]
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