1i1q

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1i1q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i1q, resolution 1.90&Aring;" /> '''STRUCTURE OF THE COO...)
Line 1: Line 1:
-
[[Image:1i1q.gif|left|200px]]<br /><applet load="1i1q" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1i1q.gif|left|200px]]<br /><applet load="1i1q" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1i1q, resolution 1.90&Aring;" />
caption="1i1q, resolution 1.90&Aring;" />
'''STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM'''<br />
'''STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM'''<br />
==Overview==
==Overview==
-
We have determined the X-ray crystal structure of the cooperative, anthranilate synthase heterotetramer from Salmonella typhimurium at 1.9 A, resolution with the allosteric inhibitor l-tryptophan bound to a, regulatory site in the TrpE subunit. Tryptophan binding orders a loop that, in turn stabilizes the inactive T state of the enzyme by restricting, closure of the active site cleft. Comparison with the structure of the, unliganded, noncooperative anthranilate synthase heterotetramer from, Sulfolobus solfataricus shows that the two homologs have completely, different quarternary structures, even though their functional dimer pairs, are structurally similar, consistent with differences in the cooperative, behavior of the enzymes. The structural model rationalizes mutational and, biochemical studies of the enzyme and establishes the structural, differences between cooperative and noncooperative anthranilate synthase, homologs.
+
We have determined the X-ray crystal structure of the cooperative anthranilate synthase heterotetramer from Salmonella typhimurium at 1.9 A resolution with the allosteric inhibitor l-tryptophan bound to a regulatory site in the TrpE subunit. Tryptophan binding orders a loop that in turn stabilizes the inactive T state of the enzyme by restricting closure of the active site cleft. Comparison with the structure of the unliganded, noncooperative anthranilate synthase heterotetramer from Sulfolobus solfataricus shows that the two homologs have completely different quarternary structures, even though their functional dimer pairs are structurally similar, consistent with differences in the cooperative behavior of the enzymes. The structural model rationalizes mutational and biochemical studies of the enzyme and establishes the structural differences between cooperative and noncooperative anthranilate synthase homologs.
==About this Structure==
==About this Structure==
-
1I1Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with TRP as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I1Q OCA].
+
1I1Q is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Salmonella_typhimurium Salmonella typhimurium] with <scene name='pdbligand=TRP:'>TRP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Anthranilate_synthase Anthranilate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.3.27 4.1.3.27] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I1Q OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Salmonella typhimurium]]
[[Category: Salmonella typhimurium]]
-
[[Category: Eck, M.J.]]
+
[[Category: Eck, M J.]]
-
[[Category: Morollo, A.A.]]
+
[[Category: Morollo, A A.]]
[[Category: TRP]]
[[Category: TRP]]
[[Category: tryptophan biosynthesis]]
[[Category: tryptophan biosynthesis]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:58:50 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:07:09 2008''

Revision as of 11:07, 21 February 2008


1i1q, resolution 1.90Å

Drag the structure with the mouse to rotate

STRUCTURE OF THE COOPERATIVE ALLOSTERIC ANTHRANILATE SYNTHASE FROM SALMONELLA TYPHIMURIUM

Overview

We have determined the X-ray crystal structure of the cooperative anthranilate synthase heterotetramer from Salmonella typhimurium at 1.9 A resolution with the allosteric inhibitor l-tryptophan bound to a regulatory site in the TrpE subunit. Tryptophan binding orders a loop that in turn stabilizes the inactive T state of the enzyme by restricting closure of the active site cleft. Comparison with the structure of the unliganded, noncooperative anthranilate synthase heterotetramer from Sulfolobus solfataricus shows that the two homologs have completely different quarternary structures, even though their functional dimer pairs are structurally similar, consistent with differences in the cooperative behavior of the enzymes. The structural model rationalizes mutational and biochemical studies of the enzyme and establishes the structural differences between cooperative and noncooperative anthranilate synthase homologs.

About this Structure

1I1Q is a Protein complex structure of sequences from Salmonella typhimurium with as ligand. Active as Anthranilate synthase, with EC number 4.1.3.27 Full crystallographic information is available from OCA.

Reference

Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium., Morollo AA, Eck MJ, Nat Struct Biol. 2001 Mar;8(3):243-7. PMID:11224570

Page seeded by OCA on Thu Feb 21 13:07:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools