1yon: Difference between revisions

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[[Image:1yon.gif|left|200px]]
{{Seed}}
[[Image:1yon.png|left|200px]]


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{{STRUCTURE_1yon|  PDB=1yon  |  SCENE=  }}  
{{STRUCTURE_1yon|  PDB=1yon  |  SCENE=  }}  


'''Escherichia coli ketopantoate reductase in complex with 2-monophosphoadenosine-5'-diphosphate'''
===Escherichia coli ketopantoate reductase in complex with 2-monophosphoadenosine-5'-diphosphate===




==Overview==
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The crystal structure of Escherichia coli ketopantoate reductase in complex with 2'-monophosphoadenosine 5'-diphosphoribose, a fragment of NADP+ that lacks the nicotinamide ring, is reported. The ligand is bound at the enzyme active site in the opposite orientation to that observed for NADP+, with the adenine ring occupying the lipophilic nicotinamide pocket. Isothermal titration calorimetry with R31A and N98A mutants of the enzyme is used to show that the unusual ;reversed binding mode' observed in the crystal is triggered by changes in the protonation of binding groups at low pH. This research has important implications for fragment-based approaches to drug design, namely that the crystallization conditions and the chemical modification of ligands can have unexpected effects on the binding modes.
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{{ABSTRACT_PUBMED_17242510}}


==About this Structure==
==About this Structure==
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[[Category: Pantothenate pathway]]
[[Category: Pantothenate pathway]]
[[Category: Secondary alcohol dehydrogenase]]
[[Category: Secondary alcohol dehydrogenase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:35:19 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:49:25 2008''

Revision as of 12:49, 28 July 2008

File:1yon.png

Template:STRUCTURE 1yon

Escherichia coli ketopantoate reductase in complex with 2-monophosphoadenosine-5'-diphosphate

Template:ABSTRACT PUBMED 17242510

About this Structure

1YON is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

pH-tuneable binding of 2'-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study., Ciulli A, Lobley CM, Tuck KL, Smith AG, Blundell TL, Abell C, Acta Crystallogr D Biol Crystallogr. 2007 Feb;63(Pt 2):171-8. Epub 2007, Jan 16. PMID:17242510

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