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.


2pza

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2pza.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2pza.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2pza| PDB=2pza | SCENE= }}
{{STRUCTURE_2pza| PDB=2pza | SCENE= }}
-
'''NAD+ Synthetase from Bacillus anthracis with AMP + PPi and Mg2+'''
+
===NAD+ Synthetase from Bacillus anthracis with AMP + PPi and Mg2+===
-
==Overview==
+
<!--
-
The crystal structures of NH(3)-dependent NAD+ synthetase from Bacillus anthracis as the apoenzyme (1.9 A), in complex with the natural catalytic products AMP and pyrophosphate (2.4 A) and in complex with the substrate analog adenosine 5'-(alpha,beta-methylene)triphosphate (2.0 A) have been determined. NAD+ synthetase catalyzes the last step in the biosynthesis of the vitally important cofactor NAD+. In comparison to other NAD+ synthetase crystal structures, the C-terminal His-tagged end of the apoenzyme adopts a novel helical conformation, causing significant compensatory changes in the region. The structural accommodations observed in B. anthracis NAD+ synthetase are remarkable in the absence of adverse affects on enzyme activity. They also illustrate a rare example of the influence of a non-native C-terminal His-tag extension on the structure of a native protein. In contrast to the apoenzyme, when AMP and pyrophosphate or adenosine 5'-(alpha,beta-methylene)triphosphate are bound, the C-terminus adopts a conformation that allows ATP binding and overall the structure then resembles other NAD+ synthetase structures. The structures of NAD+ synthetase complexes from B. anthracis are compared with published X-ray crystal structures of the enzyme from B. subtilis, Escherichia coli and Helicobacter pylori. These comparisons support the novel observation that P1 and P2 loop ordering is not a consequence of crystal contacts but rather a consequence of intrinsic intramolecular interactions within the ordered subunit.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17642516}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17642516 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17642516}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Ligase]]
[[Category: Ligase]]
[[Category: Nad+ synthetase]]
[[Category: Nad+ synthetase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:03:13 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:09:24 2008''

Revision as of 07:09, 28 July 2008

Template:STRUCTURE 2pza

NAD+ Synthetase from Bacillus anthracis with AMP + PPi and Mg2+

Template:ABSTRACT PUBMED 17642516

About this Structure

2PZA is a Single protein structure of sequence from Bacillus anthracis. Full crystallographic information is available from OCA.

Reference

Structural adaptation of an interacting non-native C-terminal helical extension revealed in the crystal structure of NAD+ synthetase from Bacillus anthracis., McDonald HM, Pruett PS, Deivanayagam C, Protasevich II, Carson WM, DeLucas LJ, Brouillette WJ, Brouillette CG, Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):891-905. Epub 2007, Jul 17. PMID:17642516

Page seeded by OCA on Mon Jul 28 10:09:24 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools