1h05: Difference between revisions

Revision as of 06:24, 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:1h05.png

Template:STRUCTURE 1h05

3-DEHYDROQUINATE DEHYDRATASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SULPHATE3-DEHYDROQUINATE DEHYDRATASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SULPHATE

Template:ABSTRACT PUBMED 12387860

About this StructureAbout this Structure

1H05 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

ReferenceReference

Specificity of substrate recognition by type II dehydroquinases as revealed by binding of polyanions., Evans LD, Roszak AW, Noble LJ, Robinson DA, Chalk PA, Matthews JL, Coggins JR, Price NC, Lapthorn AJ, FEBS Lett. 2002 Oct 23;530(1-3):24-30. PMID:12387860

Page seeded by OCA on Tue Jul 1 06:24:10 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1h05.gif|left|200px]]
+{{Seed}}
+[[Image:1h05.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1h05|  PDB=1h05  |  SCENE=  }}
-'''3-DEHYDROQUINATE DEHYDRATASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SULPHATE'''
+===3-DEHYDROQUINATE DEHYDRATASE FROM MYCOBACTERIUM TUBERCULOSIS IN COMPLEX WITH SULPHATE===
-==Overview==
+<!--
-The interactions between the polyanionic ligands phosphate and sulphate and the type II dehydroquinases from Streptomyces coelicolor and Mycobacterium tuberculosis have been characterised using a combination of structural and kinetic methods. From both approaches, it is clear that interactions are more complex in the case of the latter enzyme. The data provide new insights into the differences between the two enzymes in terms of substrate recognition and catalytic efficiency and may also explain the relative potencies of rationally designed inhibitors. An improved route to the synthesis of the substrate 3-dehydroquinic acid (dehydroquinate) is described.
+The line below this paragraph, {{ABSTRACT_PUBMED_12387860}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12387860 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12387860}}
 ==About this Structure==
@@ Line 31: / Line 35: @@
 [[Category: Lyase]]
 [[Category: Shikimate pathway]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 18:14:46 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 06:24:10 2008''