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.


1gsj

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gsj.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1gsj.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1gsj| PDB=1gsj | SCENE= }}
{{STRUCTURE_1gsj| PDB=1gsj | SCENE= }}
-
'''SELENOMETHIONINE SUBSTITUTED N-ACETYL-L-GLUTAMATE KINASE FROM ESCHERICHIA COLI COMPLEXED WITH ITS SUBSTRATE N-ACETYL-L-GLUTAMATE AND ITS SUBSTRATE ANALOG AMPPNP'''
+
===SELENOMETHIONINE SUBSTITUTED N-ACETYL-L-GLUTAMATE KINASE FROM ESCHERICHIA COLI COMPLEXED WITH ITS SUBSTRATE N-ACETYL-L-GLUTAMATE AND ITS SUBSTRATE ANALOG AMPPNP===
-
==Overview==
+
<!--
-
N-Acetyl-L-glutamate kinase (NAGK), a member of the amino acid kinase family, catalyzes the second and frequently controlling step of arginine synthesis. The Escherichia coli NAGK crystal structure to 1.5 A resolution reveals a 258-residue subunit homodimer nucleated by a central 16-stranded molecular open beta sheet sandwiched between alpha helices. In each subunit, AMPPNP, as an alphabetagamma-phosphate-Mg2+ complex, binds along the sheet C edge, and N-acetyl-L-glutamate binds near the dyadic axis with its gamma-COO- aligned at short distance from the gamma-phosphoryl, indicating associative phosphoryl transfer assisted by: (1) Mg2+ complexation; (2) the positive charges on Lys8, Lys217, and on two helix dipoles; and (3) by hydrogen bonding with the y-phosphate. The structural resemblance with carbamate kinase and the alignment of the sequences suggest that NAGK is a structural and functional prototype for the amino acid kinase family, which differs from other acylphosphate-making devices represented by phosphoglycerate kinase, acetate kinase, and biotin carboxylase.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12005432}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12005432 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12005432}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Protein crystallography]]
[[Category: Protein crystallography]]
[[Category: Selenomethionine]]
[[Category: Selenomethionine]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:57:19 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:00:15 2008''

Revision as of 03:00, 1 July 2008

Image:1gsj.png

Template:STRUCTURE 1gsj

SELENOMETHIONINE SUBSTITUTED N-ACETYL-L-GLUTAMATE KINASE FROM ESCHERICHIA COLI COMPLEXED WITH ITS SUBSTRATE N-ACETYL-L-GLUTAMATE AND ITS SUBSTRATE ANALOG AMPPNP

Template:ABSTRACT PUBMED 12005432

About this Structure

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

Reference

Structure of acetylglutamate kinase, a key enzyme for arginine biosynthesis and a prototype for the amino acid kinase enzyme family, during catalysis., Ramon-Maiques S, Marina A, Gil-Ortiz F, Fita I, Rubio V, Structure. 2002 Mar;10(3):329-42. PMID:12005432

Page seeded by OCA on Tue Jul 1 06:00:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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