1ahc: Difference between revisions

Revision as of 16:51, 30 June 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:1ahc.png

Template:STRUCTURE 1ahc

THE N-GLYCOSIDASE MECHANISM OF RIBOSOME-INACTIVATING PROTEINS IMPLIED BY CRYSTAL STRUCTURES OF ALPHA-MOMORCHARINTHE N-GLYCOSIDASE MECHANISM OF RIBOSOME-INACTIVATING PROTEINS IMPLIED BY CRYSTAL STRUCTURES OF ALPHA-MOMORCHARIN

Template:ABSTRACT PUBMED 8075985

About this StructureAbout this Structure

1AHC is a Single protein structure of sequence from Momordica charantia. Full crystallographic information is available from OCA.

ReferenceReference

The N-glycosidase mechanism of ribosome-inactivating proteins implied by crystal structures of alpha-momorcharin., Ren J, Wang Y, Dong Y, Stuart DI, Structure. 1994 Jan 15;2(1):7-16. PMID:8075985

Page seeded by OCA on Mon Jun 30 16:51:09 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1ahc.gif|left|200px]]
+{{Seed}}
+[[Image:1ahc.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1ahc|  PDB=1ahc  |  SCENE=  }}
-'''THE N-GLYCOSIDASE MECHANISM OF RIBOSOME-INACTIVATING PROTEINS IMPLIED BY CRYSTAL STRUCTURES OF ALPHA-MOMORCHARIN'''
+===THE N-GLYCOSIDASE MECHANISM OF RIBOSOME-INACTIVATING PROTEINS IMPLIED BY CRYSTAL STRUCTURES OF ALPHA-MOMORCHARIN===
-==Overview==
+<!--
-BACKGROUND: alpha-Momorcharin (alpha MMC) is a type I ribosome-inactivating protein. It inhibits protein synthesis by hydrolytically removing a specific adenine residue from a highly conserved, single-stranded loop of rRNA. RESULTS: Here we describe the determination and refinement of the crystal structures of alpha MMC in the native state and in complexes with the product, adenine, and a substrate analogue, formycin 5'-monophosphate (FMP) at high resolution. Both adenine and the base of FMP are tightly bound; the ribose of bound FMP adopts a strained, high-energy conformation, which may mimic the structure of the transition state. CONCLUSIONS: These structures indicate that residues Tyr70, Glu160 and Arg163 of alpha MMC are the most critical for catalysis. We propose that the strained conformation of the ribose in the target adenosine weakens the glycoside bond. Partial protonation mediated by Arg163 then facilitates N-glycoside bond cleavage, leading to the formation of an oxycarbonium ion intermediate which is stabilized by the negatively-charged Glu160. Tyr70 adopts subtly different conformations in the three structures implying that it may be important in substrate recognition and perhaps catalysis.
+The line below this paragraph, {{ABSTRACT_PUBMED_8075985}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8075985 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8075985}}
 ==About this Structure==
@@ Line 28: / Line 32: @@
 [[Category: Wang, Y.]]
 [[Category: Glycosidase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 10:16:16 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 16:51:09 2008''