1hfb
From Proteopedia
(New page: 200px<br /> <applet load="1hfb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hfb, resolution 1.9Å" /> '''CRYSTAL STRUCTURE OF...) |
|||
| Line 8: | Line 8: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1HFB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]] with PEP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.15 4.1.2.15]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HFB OCA]]. | + | 1HFB is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]] with PEP as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/Transferred_entry:_2.5.1.54 Transferred entry: 2.5.1.54]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.15 4.1.2.15]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HFB OCA]]. |
==Reference== | ==Reference== | ||
| Line 14: | Line 14: | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| + | [[Category: Transferred entry: 2.5.1.54]] | ||
[[Category: Braus, G.H.]] | [[Category: Braus, G.H.]] | ||
[[Category: Hartmann, M.]] | [[Category: Hartmann, M.]] | ||
| Line 21: | Line 22: | ||
[[Category: lyase]] | [[Category: lyase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 13:49:21 2007'' |
Revision as of 11:44, 30 October 2007
|
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
Page seeded by OCA on Tue Oct 30 13:49:21 2007
