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.


1n2e

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1n2e.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1n2e.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1n2e| PDB=1n2e | SCENE= }}
{{STRUCTURE_1n2e| PDB=1n2e | SCENE= }}
-
'''Crystal Structure of a Pantothenate Synthetase from M. tuberculosis in complex with AMPCPP and pantoate'''
+
===Crystal Structure of a Pantothenate Synthetase from M. tuberculosis in complex with AMPCPP and pantoate===
-
==Overview==
+
<!--
-
Pantothenate biosynthesis is essential for the virulence of Mycobacterium tuberculosis, and this pathway thus presents potential drug targets against tuberculosis. We determined the crystal structure of pantothenate synthetase (PS) from M. tuberculosis, and its complexes with AMPCPP, pantoate, and a reaction intermediate, pantoyl adenylate, with resolutions from 1.6 to 2 A. PS catalyzes the ATP-dependent condensation of pantoate and beta-alanine to form pantothenate. Its structure reveals a dimer, and each subunit has two domains with tight association between domains. The active-site cavity is on the N-terminal domain, partially covered by the C-terminal domain. One wall of the active site cavity is flexible, which allows the bulky AMPCPP to diffuse into the active site to nearly full occupancy when crystals are soaked in solutions containing AMPCPP. Crystal structures of the complexes with AMPCPP and pantoate indicate that the enzyme binds ATP and pantoate tightly in the active site, and brings the carboxyl oxygen of pantoate near the alpha-phosphorus atom of ATP for an in-line nucleophilic attack. When crystals were soaked with, or grown in the presence of, both ATP and pantoate, a reaction intermediate, pantoyl adenylate, is found in the active site. The flexible wall of the active site cavity becomes ordered when the intermediate is in the active site, thus protecting it from being hydrolyzed. Binding of beta-alanine can occur only after pantoyl adenylate is formed inside the active site cavity. The tight binding of the intermediate pantoyl adenylate suggests that nonreactive analogs of pantoyl adenylate may be inhibitors of the PS enzyme with high affinity and specificity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12717031}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12717031 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12717031}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Tb structural genomics consortium]]
[[Category: Tb structural genomics consortium]]
[[Category: Tbsgc]]
[[Category: Tbsgc]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:00:15 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:45:45 2008''

Revision as of 10:45, 27 July 2008

Image:1n2e.png

Template:STRUCTURE 1n2e

Crystal Structure of a Pantothenate Synthetase from M. tuberculosis in complex with AMPCPP and pantoate

Template:ABSTRACT PUBMED 12717031

About this Structure

1N2E is a Single protein structure of sequence from Mycobacterium tuberculosis. Full crystallographic information is available from OCA.

Reference

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 Sun Jul 27 13:45:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1n2e"
Personal tools