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.


1kkm

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kkm.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1kkm.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kkm| PDB=1kkm | SCENE= }}
{{STRUCTURE_1kkm| PDB=1kkm | SCENE= }}
-
'''L.casei HprK/P in complex with B.subtilis P-Ser-HPr'''
+
===L.casei HprK/P in complex with B.subtilis P-Ser-HPr===
-
==Overview==
+
<!--
-
HPr kinase/phosphorylase (HprK/P) controls the phosphorylation state of the phosphocarrier protein HPr and regulates the utilization of carbon sources by Gram-positive bacteria. It catalyzes both the ATP-dependent phosphorylation of Ser-46 of HPr and its dephosphorylation by phosphorolysis. The latter reaction uses inorganic phosphate as substrate and produces pyrophosphate. We present here two crystal structures of a complex of the catalytic domain of Lactobacillus casei HprK/P with Bacillus subtilis HPr, both at 2.8-A resolution. One of the structures was obtained in the presence of excess pyrophosphate, reversing the phosphorolysis reaction and contains serine-phosphorylated HPr. The complex has six HPr molecules bound to the hexameric kinase. Two adjacent enzyme subunits are in contact with each HPr molecule, one through its active site and the other through its C-terminal helix. In the complex with serine-phosphorylated HPr, a phosphate ion is in a position to perform a nucleophilic attack on the phosphoserine. Although the mechanism of the phosphorylation reaction resembles that of eukaryotic protein kinases, the dephosphorylation by inorganic phosphate is unique to the HprK/P family of kinases. This study provides the structure of a protein kinase in complex with its protein substrate, giving insights into the chemistry of the phospho-transfer reactions in both directions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12359875}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12359875 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12359875}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Protein kinase]]
[[Category: Protein kinase]]
[[Category: Protein/protein interaction]]
[[Category: Protein/protein interaction]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:51:23 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:28:52 2008''

Revision as of 07:28, 2 July 2008

Image:1kkm.png

Template:STRUCTURE 1kkm

L.casei HprK/P in complex with B.subtilis P-Ser-HPr

Template:ABSTRACT PUBMED 12359875

About this Structure

1KKM is a Protein complex structure of sequences from Bacillus subtilis and Lactobacillus casei. Full crystallographic information is available from OCA.

Reference

X-ray structure of a bifunctional protein kinase in complex with its protein substrate HPr., Fieulaine S, Morera S, Poncet S, Mijakovic I, Galinier A, Janin J, Deutscher J, Nessler S, Proc Natl Acad Sci U S A. 2002 Oct 15;99(21):13437-41. Epub 2002 Oct 1. PMID:12359875

Page seeded by OCA on Wed Jul 2 10:28:52 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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