1hfb: Difference between revisions

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


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{{STRUCTURE_1hfb|  PDB=1hfb  |  SCENE=  }}  
{{STRUCTURE_1hfb|  PDB=1hfb  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE TYROSINE-REGULATED 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE SYNTHASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH PHOSPHOENOLPYRUVATE'''
===CRYSTAL STRUCTURE OF THE TYROSINE-REGULATED 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE SYNTHASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH PHOSPHOENOLPYRUVATE===




==Overview==
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The betaalpha barrel is the common protein fold of numerous enzymes and was proposed recently to be the result of gene duplication and fusion of an ancient half-barrel. The initial enzyme of shikimate biosynthesis possesses the additional feature of feedback regulation. The crystal structure and kinetic studies on chimera and mutant proteins of yeast 3-deoxy-d-arabino-heptulosonate-7-phosphate (DAHP) synthase from Saccharomyces cerevisiae inhibited by phenylalanine (Aro3p) and DAHP synthase S. cerevisiae inhibited by tyrosine (Aro4p) give insight into important regions for regulation in the enzyme: The loop, which is connecting the two half-barrels, and structural elements added to the barrel are prerequisites for regulation and form a cavity on the N-terminal side of the betaalpha barrel. In the cavity of Aro4p at position 226 is a glycine residue, which is highly conserved in all other tyrosine-regulated DAHP synthases as well. Sequence alignments with phenylalanine-regulated DAHP synthases including Aro3p show a highly conserved serine residue at this position. An exchange of glycine to serine and vice versa leads to a complete change in the regulation pattern. Therefore the evolution of these differently feedback-inhibited isoenzymes required gene duplication and a single mutation within the internal extra element. Numerous additional amino acid substitutions present in the contemporary isoenzymes are irrelevant for regulation and occurred independently.
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{{ABSTRACT_PUBMED_12540830}}


==About this Structure==
==About this Structure==
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[[Category: Beta-alpha-barrel]]
[[Category: Beta-alpha-barrel]]
[[Category: Lyase]]
[[Category: Lyase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:47:27 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 08:06:28 2008''

Revision as of 05:06, 1 July 2008

File:1hfb.png

Template:STRUCTURE 1hfb

CRYSTAL STRUCTURE OF THE TYROSINE-REGULATED 3-DEOXY-D-ARABINO-HEPTULOSONATE-7-PHOSPHATE SYNTHASE FROM SACCHAROMYCES CEREVISIAE COMPLEXED WITH PHOSPHOENOLPYRUVATE

Template:ABSTRACT PUBMED 12540830

About this Structure

1HFB is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Evolution of feedback-inhibited beta /alpha barrel isoenzymes by gene duplication and a single mutation., Hartmann M, Schneider TR, Pfeil A, Heinrich G, Lipscomb WN, Braus GH, Proc Natl Acad Sci U S A. 2003 Feb 4;100(3):862-7. Epub 2003 Jan 22. PMID:12540830

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