1c8v: Difference between revisions

Revision as of 20:22, 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:1c8v.png

Template:STRUCTURE 1c8v

CRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE WITH THE TRANSITION STATE ANALOGUE INHIBITOR 4-(2-HYDROXYPHENYLTHIO)-BUTYLPHOSPHONIC ACIDCRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE WITH THE TRANSITION STATE ANALOGUE INHIBITOR 4-(2-HYDROXYPHENYLTHIO)-BUTYLPHOSPHONIC ACID

Template:ABSTRACT PUBMED 10504236

About this StructureAbout this Structure

1C8V is a Protein complex structure of sequences from Salmonella typhimurium. Full crystallographic information is available from OCA.

ReferenceReference

Crystallographic studies of phosphonate-based alpha-reaction transition-state analogues complexed to tryptophan synthase., Sachpatzidis A, Dealwis C, Lubetsky JB, Liang PH, Anderson KS, Lolis E, Biochemistry. 1999 Sep 28;38(39):12665-74. PMID:10504236

Page seeded by OCA on Mon Jun 30 20:22:50 2008

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

OCA

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-[[Image:1c8v.gif|left|200px]]
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 {{STRUCTURE_1c8v|  PDB=1c8v  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE WITH THE TRANSITION STATE ANALOGUE INHIBITOR 4-(2-HYDROXYPHENYLTHIO)-BUTYLPHOSPHONIC ACID'''
+===CRYSTAL STRUCTURE OF THE COMPLEX OF BACTERIAL TRYPTOPHAN SYNTHASE WITH THE TRANSITION STATE ANALOGUE INHIBITOR 4-(2-HYDROXYPHENYLTHIO)-BUTYLPHOSPHONIC ACID===
-==Overview==
+<!--
-In an effort to use a structure-based approach for the design of new herbicides, the crystal structures of complexes of tryptophan synthase with a series of phosphonate enzyme inhibitors were determined at 2.3 A or higher resolution. These inhibitors were designed to mimic the transition state formed during the alpha-reaction of the enzyme and, as expected, have affinities much greater than that of the natural substrate indole-3-glycerol phosphate or its nonhydrolyzable analogue indole propanol phosphate (IPP). These inhibitors are ortho-substituted arylthioalkylphosphonate derivatives that have an sp(3)-hybridized sulfur atom, designed to mimic the putative tetrahedral transition state at the C3 atom of the indole, and lack the C2 atom to allow for higher conformational flexibility. Overall, the inhibitors bind in a fashion similar to that of IPP. Glu-49 and Phe-212 are the two active site residues whose conformation changes upon inhibitor binding. A very short hydrogen bond between a phosphonate oxygen and the Ser-235 hydroxyl oxygen may be responsible for stabilization of the enzyme-inhibitor complexes. Implications for the mechanism of catalysis as well as directions for more potent inhibitors are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_10504236}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10504236 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_10504236}}
 ==About this Structure==
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 [[Category: Enzyme-inhibitor complex]]
 [[Category: Lyase]]
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