2mas: Difference between revisions

Revision as of 15:27, 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:2mas.png

Template:STRUCTURE 2mas

PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITORPURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR

Template:ABSTRACT PUBMED 9572842

About this StructureAbout this Structure

2MAS is a Single protein structure of sequence from Crithidia fasciculata. Full crystallographic information is available from OCA.

ReferenceReference

Trypanosomal nucleoside hydrolase. A novel mechanism from the structure with a transition-state inhibitor., Degano M, Almo SC, Sacchettini JC, Schramm VL, Biochemistry. 1998 May 5;37(18):6277-85. PMID:9572842

Page seeded by OCA on Mon Jul 28 15:27:24 2008

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

OCA

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-'''PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR'''
+===PURINE NUCLEOSIDE HYDROLASE WITH A TRANSITION STATE INHIBITOR===
-==Overview==
+<!--
-Nucleoside N-ribohydrolases are targets for disruption of purine salvage in the protozoan parasites. The structure of a trypanosomal N-ribohydrolase in complex with a transition-state inhibitor is reported at 2.3 A resolution. The nonspecific nucleoside hydrolase from Crithidia fasciculata cocrystallized with p-aminophenyliminoribitol reveals tightly bound Ca2+ as a catalytic site ligand. The complex with the transition-state inhibitor is characterized by (1) large protein conformational changes to create a hydrophobic leaving group site (2) C3'-exo geometry for the inhibitor, typical of a ribooxocarbenium ion (3) stabilization of the ribooxocarbenium analogue between the neighboring group 5'-hydroxyl and bidentate hydrogen bonds to Asn168; and (4) octacoordinate Ca2+ orients a catalytic site water and is liganded to two hydroxyls of the inhibitor. The mechanism is ribooxocarbenium stabilization with weak leaving group activation and is a departure from glucohydrolases which use paired carboxylates to achieve the transition state.
+The line below this paragraph, {{ABSTRACT_PUBMED_9572842}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9572842 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_9572842}}
 ==About this Structure==
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 [[Category: Purine nucleoside hydrolase]]
 [[Category: Uridine]]
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