1hfb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1hfb.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1hfb.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{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==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12540830}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12540830 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12540830}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[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

Image: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

Page seeded by OCA on Tue Jul 1 08:06:28 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1hfb"
Personal tools