2a88: Difference between revisions

Revision as of 20:52, 28 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:2a88.png

Template:STRUCTURE 2a88

Crystal structure of A Pantothenate synthetase, apo enzyme in C2 space groupCrystal structure of A Pantothenate synthetase, apo enzyme in C2 space group

Template:ABSTRACT PUBMED 16460002

About this StructureAbout this Structure

2A88 is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the pantothenate synthetase from Mycobacterium tuberculosis, snapshots of the enzyme in action., Wang S, Eisenberg D, Biochemistry. 2006 Feb 14;45(6):1554-61. PMID:16460002

Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate., Wang S, Eisenberg D, Protein Sci. 2003 May;12(5):1097-108. PMID:12717031

Page seeded by OCA on Mon Jul 28 20:52:47 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2a88.gif|left|200px]]
+{{Seed}}
+[[Image:2a88.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2a88|  PDB=2a88  |  SCENE=  }}
-'''Crystal structure of A Pantothenate synthetase, apo enzyme in C2 space group'''
+===Crystal structure of A Pantothenate synthetase, apo enzyme in C2 space group===
-==Overview==
+<!--
-Pantothenate synthetase (PS) from Mycobacterium tuberculosis represents a potential target for antituberculosis drugs. PS catalyzes the ATP-dependent condensation of pantoate and beta-alanine to form pantothenate. Previously, we determined the crystal structure of PS from M. tuberculosis and its complexes with AMPCPP, pantoate, and pantoyl adenylate. Here, we describe the crystal structure of this enzyme complexed with AMP and its last substrate, beta-alanine, and show that the phosphate group of AMP serves as an anchor for the binding of beta-alanine. This structure confirms that binding of beta-alanine in the active site cavity can occur only after formation of the pantoyl adenylate intermediate. A new crystal form was also obtained; it displays the flexible wall of the active site cavity in a conformation incapable of binding pantoate. Soaking of this crystal form with ATP and pantoate gives a fully occupied complex of PS with ATP. Crystal structures of these complexes with substrates, the reaction intermediate, and the reaction product AMP provide a step-by-step view of the PS-catalyzed reaction. A detailed reaction mechanism and its implications for inhibitor design are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_16460002}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16460002 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16460002}}
 ==About this Structure==
@@ Line 20: / Line 24: @@
 ==Reference==
 Crystal structure of the pantothenate synthetase from Mycobacterium tuberculosis, snapshots of the enzyme in action., Wang S, Eisenberg D, Biochemistry. 2006 Feb 14;45(6):1554-61. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16460002 16460002]
+Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate., Wang S, Eisenberg D, Protein Sci. 2003 May;12(5):1097-108. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12717031 12717031]
 [[Category: Mycobacterium tuberculosis]]
 [[Category: Pantoate--beta-alanine ligase]]
@@ Line 33: / Line 39: @@
 [[Category: Tb structural genomics consortium]]
 [[Category: Tbsgc]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 18:43:59 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 20:52:47 2008''