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.


2jg1

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2jg1.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2jg1.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2jg1| PDB=2jg1 | SCENE= }}
{{STRUCTURE_2jg1| PDB=2jg1 | SCENE= }}
-
'''STRUCTURE OF STAPHYLOCOCCUS AUREUS D-TAGATOSE-6-PHOSPHATE KINASE WITH COFACTOR AND SUBSTRATE'''
+
===STRUCTURE OF STAPHYLOCOCCUS AUREUS D-TAGATOSE-6-PHOSPHATE KINASE WITH COFACTOR AND SUBSTRATE===
-
==Overview==
+
<!--
-
High resolution structures of Staphylococcus aureus d-tagatose-6-phosphate kinase (LacC) in two crystal forms are herein reported. The structures define LacC in apoform, in binary complexes with ADP or the co-factor analogue AMP-PNP, and in a ternary complex with AMP-PNP and D-tagatose-6-phosphate. The tertiary structure of the LacC monomer, which is closely related to other members of the pfkB subfamily of carbohydrate kinases, is composed of a large alpha/beta core domain and a smaller, largely beta "lid." Four extended polypeptide segments connect these two domains. Dimerization of LacC occurs via interactions between lid domains, which come together to form a beta-clasp structure. Residues from both subunits contribute to substrate binding. LacC adopts a closed structure required for phosphoryl transfer only when both substrate and co-factor are bound. A reaction mechanism similar to that used by other phosphoryl transferases is proposed, although unusually, when both substrate and co-factor are bound to the enzyme two Mg(2+) ions are observed in the active site. A new motif of amino acid sequence conservation common to the pfkB subfamily of carbohydrate kinases is identified.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17459874}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17459874 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17459874}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Phosphoryl transfer]]
[[Category: Phosphoryl transfer]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 08:51:25 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:29:56 2008''

Revision as of 05:30, 29 July 2008

Image:2jg1.png

Template:STRUCTURE 2jg1

STRUCTURE OF STAPHYLOCOCCUS AUREUS D-TAGATOSE-6-PHOSPHATE KINASE WITH COFACTOR AND SUBSTRATE

Template:ABSTRACT PUBMED 17459874

About this Structure

2JG1 is a Single protein structure of sequence from Staphylococcus aureus. Full crystallographic information is available from OCA.

Reference

Structures of Staphylococcus aureus D-tagatose-6-phosphate kinase implicate domain motions in specificity and mechanism., Miallau L, Hunter WN, McSweeney SM, Leonard GA, J Biol Chem. 2007 Jul 6;282(27):19948-57. Epub 2007 Apr 25. PMID:17459874

Page seeded by OCA on Tue Jul 29 08:29:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2jg1"
Personal tools