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.


2hro

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hro.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2hro.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hro| PDB=2hro | SCENE= }}
{{STRUCTURE_2hro| PDB=2hro | SCENE= }}
-
'''Structure of the full-lenght Enzyme I of the PTS system from Staphylococcus carnosus'''
+
===Structure of the full-lenght Enzyme I of the PTS system from Staphylococcus carnosus===
-
==Overview==
+
<!--
-
Enzyme I (EI) is the phosphoenolpyruvate (PEP)-protein phosphotransferase at the entry point of the PEP-dependent sugar phosphotransferase system, which catalyzes carbohydrate uptake into bacterial cells. In the first step of this pathway EI phosphorylates the heat-stable phospho carrier protein at His-15 using PEP as a phosphoryl donor in a reaction that requires EI dimerization and autophosphorylation at His-190. The structure of the full-length protein from Staphylococcus carnosus at 2.5A reveals an extensive interaction surface between two molecules in adjacent asymmetric units. Structural comparison with related domains indicates that this surface represents the biochemically relevant contact area of dimeric EI. Each monomer has an extended configuration with the phosphohistidine and heat-stable phospho carrier protein-binding domains clearly separated from the C-terminal dimerization and PEP-binding region. The large distance of more than 35A between the active site His-190 and the PEP binding site suggests that large conformational changes must occur during the process of autophosphorylation, as has been proposed for the structurally related enzyme pyruvate phosphate dikinase. Our structure for the first time offers a framework to analyze a large amount of research in the context of the full-length model.
+
The line below this paragraph, {{ABSTRACT_PUBMED_16867985}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16867985 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16867985}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Pt]]
[[Category: Pt]]
[[Category: Sugar transport]]
[[Category: Sugar transport]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:37:53 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:35:45 2008''

Revision as of 15:35, 27 July 2008

Image:2hro.png

Template:STRUCTURE 2hro

Structure of the full-lenght Enzyme I of the PTS system from Staphylococcus carnosus

Template:ABSTRACT PUBMED 16867985

About this Structure

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

Reference

Structure of the full-length enzyme I of the phosphoenolpyruvate-dependent sugar phosphotransferase system., Marquez J, Reinelt S, Koch B, Engelmann R, Hengstenberg W, Scheffzek K, J Biol Chem. 2006 Oct 27;281(43):32508-15. Epub 2006 Jul 25. PMID:16867985

Page seeded by OCA on Sun Jul 27 18:35:45 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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