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.


1zym

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1zym.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1zym.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1zym| PDB=1zym | SCENE= }}
{{STRUCTURE_1zym| PDB=1zym | SCENE= }}
-
'''AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI'''
+
===AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI===
-
==Overview==
+
<!--
-
BACKGROUND: The bacterial phosphoenolpyruvate (PEP): sugar phosphotransferase system (PTS) transports exogenous hexose sugars through the membrane and tightly couples transport with phosphoryl transfer from PEP to the sugar via several phosphoprotein intermediates. The phosphate group is first transferred to enzyme I, second to the histidine-containing phosphocarrier protein HPr, and then to one of a number of sugar-specific enzymes II. The structures of several HPrs and enzymes IIA are known. Here we report the structure of the N-terminal half of enzyme I from Escherichia coli (EIN). RESULTS: The crystal structure of EIN (MW approximately 30 kDa) has been determined and refined at 2.5 A resolution. It has two distinct structural subdomains; one contains four alpha helices arranged as two hairpins in a claw-like conformation. The other consists of a beta sandwich containing a three-stranded antiparallel beta sheet and a four-stranded parallel beta sheet, together with three short alpha helices. Plausible models of complexes between EIN and HPr can be made without assuming major structural changes in either protein. CONCLUSIONS: The alpha/beta subdomain of EIN is topologically similar to the phosphohistidine domain of the enzyme pyruvate phosphate dikinase, which is phosphorylated by PEP on a histidyl residue but does not interact with HPr. It is therefore likely that features of this subdomain are important in the autophosphorylation of enzyme I. The helical subdomain of EIN is not found in pyruvate phosphate dikinase; this subdomain is therefore more likely to be involved in phosphoryl transfer to HPr.
+
The line below this paragraph, {{ABSTRACT_PUBMED_8805571}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 8805571 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_8805571}}
==About this Structure==
==About this Structure==
Line 26: Line 30:
[[Category: Liao, D I.]]
[[Category: Liao, D I.]]
[[Category: Phosphotransferase]]
[[Category: Phosphotransferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:14:32 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:46:04 2008''

Revision as of 20:46, 27 July 2008

Image:1zym.png

Template:STRUCTURE 1zym

AMINO TERMINAL DOMAIN OF ENZYME I FROM ESCHERICHIA COLI

Template:ABSTRACT PUBMED 8805571

About this Structure

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

Reference

The first step in sugar transport: crystal structure of the amino terminal domain of enzyme I of the E. coli PEP: sugar phosphotransferase system and a model of the phosphotransfer complex with HPr., Liao DI, Silverton E, Seok YJ, Lee BR, Peterkofsky A, Davies DR, Structure. 1996 Jul 15;4(7):861-72. PMID:8805571

Page seeded by OCA on Sun Jul 27 23:46:04 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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