1nvf: Difference between revisions

Revision as of 17:10, 27 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:1nvf.png

Template:STRUCTURE 1nvf

Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+, ADP and carbaphosphonateCrystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+, ADP and carbaphosphonate

Template:ABSTRACT PUBMED 12614613

About this StructureAbout this Structure

1NVF is a Single protein structure of sequence from Emericella nidulans. Full crystallographic information is available from OCA.

ReferenceReference

Ligand-induced conformational changes and a mechanism for domain closure in Aspergillus nidulans dehydroquinate synthase., Nichols CE, Ren J, Lamb HK, Hawkins AR, Stammers DK, J Mol Biol. 2003 Mar 14;327(1):129-44. PMID:12614613

Page seeded by OCA on Sun Jul 27 17:10:25 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1nvf.jpg|left|200px]]
+{{Seed}}
+[[Image:1nvf.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1nvf|  PDB=1nvf  |  SCENE=  }}
-'''Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+, ADP and carbaphosphonate'''
+===Crystal structure of 3-dehydroquinate synthase (DHQS) in complex with ZN2+, ADP and carbaphosphonate===
-==Overview==
+<!--
-In order to investigate systematically substrate and cofactor-induced conformational changes in the enzyme dehydroquinate synthase (DHQS), eight structures representing a series of differently liganded states have been determined in a total of six crystal forms. DHQS in the absence of the substrate analogue carbaphosphonate, either unliganded or in the presence of NAD or ADP, is in an open form where a relative rotation of 11-13 degrees between N and C-terminal domains occurs.Analysis of torsion angle difference plots between sets of structures reveals eight rearrangements that appear relevant to domain closure and a further six related to crystal packing. Overlapping 21 different copies of the individual N and C-terminal DHQS domains further reveals a series of pivot points about which these movements occur and illustrates the way in which widely separated secondary structure elements are mechanically inter-linked to form "composite elements", which propagate structural changes across large distances.This analysis has provided insight into the basis of DHQS ligand-initiated domain closure and gives rise to the proposal of an ordered sequence of events involving substrate binding, and local rearrangements within the active site that are propagated to the hinge regions, leading to closure of the active-site cleft.
+The line below this paragraph, {{ABSTRACT_PUBMED_12614613}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12614613 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12614613}}
 ==About this Structure==
@@ Line 36: / Line 40: @@
 [[Category: Lyase]]
 [[Category: Shikimate pathway]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:01:30 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:10:25 2008''