1hfb

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1hfb, resolution 1.9Å

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

Overview

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 ... [(full description)]

About this Structure

1HFB is a [Single protein] structure of sequence from [Saccharomyces cerevisiae] with PEP as [ligand]. Active as [Transferred entry: 2.5.1.54], with EC number [4.1.2.15]. Structure known Active Site: AC1. 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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