1gqn: Difference between revisions

Revision as of 05:54, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1gqn.png

Template:STRUCTURE 1gqn

NATIVE 3-DEHYDROQUINASE FROM SALMONELLA TYPHINATIVE 3-DEHYDROQUINASE FROM SALMONELLA TYPHI

Template:ABSTRACT PUBMED 11976491

About this StructureAbout this Structure

1GQN is a Single protein structure of sequence from Salmonella typhi. Full crystallographic information is available from OCA.

ReferenceReference

Comparison of different crystal forms of 3-dehydroquinase from Salmonella typhi and its implication for the enzyme activity., Lee WH, Perles LA, Nagem RA, Shrive AK, Hawkins A, Sawyer L, Polikarpov I, Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):798-804. Epub 2002, Apr 26. PMID:11976491

Page seeded by OCA on Tue Jul 1 05:54:37 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1gqn.gif|left|200px]]
+{{Seed}}
+[[Image:1gqn.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1gqn|  PDB=1gqn  |  SCENE=  }}
-'''NATIVE 3-DEHYDROQUINASE FROM SALMONELLA TYPHI'''
+===NATIVE 3-DEHYDROQUINASE FROM SALMONELLA TYPHI===
-==Overview==
+<!--
-The type I 3-dehydroquinate dehydratase (DHQase) which catalyses the reversible dehydration of 3-dehydroquinic acid to 3-dehydroshikimic acid is involved in the shikimate pathway for the biosynthesis of aromatic compounds. The shikimate pathway is absent in mammals, which makes structural information about DHQase vital for the rational design of antimicrobial drugs and herbicides. The crystallographic structure of the type I DHQase from Salmonella typhi has now been determined for the native form at 1.78 A resolution (R = 19.9%; R(free) = 24.7%). The structure of the modified enzyme to which the product has been covalently bound has also been determined but in a different crystal form (2.1 A resolution; R = 17.7%; R(free) = 24.5%). An analysis of the three available crystal forms has provided information about the physiological dimer interface. The enzyme relies upon the closure of a lid-like loop to complete its active site. As the lid-loop tends to stay in the closed position, dimerization appears to play a role in biasing the arrangement of the loop towards its open position, thus facilitating substrate access.
+The line below this paragraph, {{ABSTRACT_PUBMED_11976491}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11976491 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11976491}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: A/b barrel]]
 [[Category: Shikimate pathway]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:53:59 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 05:54:37 2008''