1k7x

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1k7x.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1k7x.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1k7x| PDB=1k7x | SCENE= }}
{{STRUCTURE_1k7x| PDB=1k7x | SCENE= }}
-
'''CRYSTAL STRUCTURE OF THE BETA-SER178PRO MUTANT OF TRYPTOPHAN SYNTHASE'''
+
===CRYSTAL STRUCTURE OF THE BETA-SER178PRO MUTANT OF TRYPTOPHAN SYNTHASE===
-
==Overview==
+
<!--
-
The catalytic activity of the pyridoxal 5'-phosphate-dependent tryptophan synthase alpha(2)beta(2) complex is allosterically regulated. The hydrogen bond between the helix betaH6 residue betaSer(178) and the loop alphaL6 residue Gly(181) was shown to be critical in ligand-induced intersubunit signaling, with the alpha-beta communication being completely lost in the mutant betaSer(178) --&gt; Pro (Marabotti, A., De Biase, D., Tramonti, A., Bettati, S., and Mozzarelli, A. (2001) J. Biol. Chem. 276, 17747-17753). The structural basis of the impaired allosteric regulation was investigated by determining the crystal structures of the mutant betaSer(178) --&gt; Pro in the absence and presence of the alpha-subunit ligands indole-3-acetylglycine and glycerol 3-phosphate. The mutation causes local and distant conformational changes especially in the beta-subunit. The ligand-free structure exhibits larger differences at the N-terminal part of helix betaH6, whereas the enzyme ligand complexes show differences at the C-terminal side. In contrast to the wild-type enzyme loop alphaL6 remains in an open conformation even in the presence of alpha-ligands. This effects the equilibrium between active and inactive conformations of the alpha-active site, altering k(cat) and K(m), and forms the structural basis for the missing allosteric communication between the alpha- and beta-subunits.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11756454}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11756454 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11756454}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Pyridoxal phosphate]]
[[Category: Pyridoxal phosphate]]
[[Category: Tryptophan biosynthesis]]
[[Category: Tryptophan biosynthesis]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:24:53 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 09:55:11 2008''

Revision as of 06:55, 2 July 2008

Image:1k7x.png

Template:STRUCTURE 1k7x

CRYSTAL STRUCTURE OF THE BETA-SER178PRO MUTANT OF TRYPTOPHAN SYNTHASE

Template:ABSTRACT PUBMED 11756454

About this Structure

1K7X is a Protein complex structure of sequences from Salmonella typhimurium. Full crystallographic information is available from OCA.

Reference

Crystal structure of the beta Ser178--> Pro mutant of tryptophan synthase. A "knock-out" allosteric enzyme., Weyand M, Schlichting I, Herde P, Marabotti A, Mozzarelli A, J Biol Chem. 2002 Mar 22;277(12):10653-60. Epub 2001 Dec 26. PMID:11756454

Page seeded by OCA on Wed Jul 2 09:55:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1k7x"
Personal tools