This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1i7q

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1i7q.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1i7q.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1i7q| PDB=1i7q | SCENE= }}
{{STRUCTURE_1i7q| PDB=1i7q | SCENE= }}
-
'''ANTHRANILATE SYNTHASE FROM S. MARCESCENS'''
+
===ANTHRANILATE SYNTHASE FROM S. MARCESCENS===
-
==Overview==
+
<!--
-
The crystal structure of anthranilate synthase (AS) from Serratia marcescens, a mesophilic bacterium, has been solved in the presence of its substrates, chorismate and glutamine, and one product, glutamate, at 1.95 A, and with its bound feedback inhibitor, tryptophan, at 2.4 A. In comparison with the AS structure from the hyperthermophile Sulfolobus solfataricus, the S. marcescens structure shows similar subunit structures but a markedly different oligomeric organization. One crystal form of the S. marcescens enzyme displays a bound pyruvate as well as a putative anthranilate (the nitrogen group is ambiguous) in the TrpE subunit. It also confirms the presence of a covalently bound glutamyl thioester intermediate in the TrpG subunit. The tryptophan-bound form reveals that the inhibitor binds at a site distinct from that of the substrate, chorismate. Bound tryptophan appears to prevent chorismate binding by a demonstrable conformational effect, and the structure reveals how occupancy of only one of the two feedback inhibition sites can immobilize the catalytic activity of both TrpE subunits. The presence of effectors in the structure provides a view of the locations of some of the amino acid residues in the active sites. Our findings are discussed in terms of the previously described AS structure of S. solfataricus, mutational data obtained from enteric bacteria, and the enzyme's mechanism of action.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11371633}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11371633 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11371633}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Chorismate binding]]
[[Category: Chorismate binding]]
[[Category: Glutamyl thioester]]
[[Category: Glutamyl thioester]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 19:40:45 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 10:32:55 2008''

Revision as of 07:32, 1 July 2008

Image:1i7q.png

Template:STRUCTURE 1i7q

ANTHRANILATE SYNTHASE FROM S. MARCESCENS

Template:ABSTRACT PUBMED 11371633

About this Structure

1I7Q is a Protein complex structure of sequences from Serratia marcescens. Full crystallographic information is available from OCA.

Reference

The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan., Spraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE, Proc Natl Acad Sci U S A. 2001 May 22;98(11):6021-6. PMID:11371633

Page seeded by OCA on Tue Jul 1 10:32:55 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1i7q"
Personal tools