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.


1v4a

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1v4a.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1v4a.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1v4a| PDB=1v4a | SCENE= }}
{{STRUCTURE_1v4a| PDB=1v4a | SCENE= }}
-
'''Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase'''
+
===Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase===
-
==Overview==
+
<!--
-
We report the crystal structure of the N-terminal domain of Escherichia coli adenylyltransferase that catalyzes the reversible nucleotidylation of glutamine synthetase (GS), a key enzyme in nitrogen assimilation. This domain (AT-N440) catalyzes the deadenylylation and subsequent activation of GS. The structure has been divided into three subdomains, two of which bear some similarity to kanamycin nucleotidyltransferase (KNT). However, the orientation of the two domains in AT-N440 differs from that in KNT. The active site of AT-N440 has been identified on the basis of structural comparisons with KNT, DNA polymerase beta, and polyadenylate polymerase. AT-N440 has a cluster of metal binding residues that are conserved in polbeta-like nucleotidyl transferases. The location of residues conserved in all ATase sequences was found to cluster around the active site. Many of these residues are very likely to play a role in catalysis, substrate binding, or effector binding.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15130478}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15130478 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15130478}}
==About this Structure==
==About this Structure==
Line 30: Line 34:
[[Category: Dna polymerase beta motif]]
[[Category: Dna polymerase beta motif]]
[[Category: Main alpha helix]]
[[Category: Main alpha helix]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 12:03:39 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:56:11 2008''

Revision as of 12:56, 28 July 2008

Image:1v4a.png

Template:STRUCTURE 1v4a

Structure of the N-terminal Domain of Escherichia coli Glutamine Synthetase adenylyltransferase

Template:ABSTRACT PUBMED 15130478

About this Structure

1V4A is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of the N-terminal domain of Escherichia coli glutamine synthetase adenylyltransferase., Xu Y, Zhang R, Joachimiak A, Carr PD, Huber T, Vasudevan SG, Ollis DL, Structure. 2004 May;12(5):861-9. PMID:15130478

Page seeded by OCA on Mon Jul 28 15:56:11 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1v4a"
Personal tools