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.


1jp3

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1jp3.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1jp3.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1jp3| PDB=1jp3 | SCENE= }}
{{STRUCTURE_1jp3| PDB=1jp3 | SCENE= }}
-
'''Structure of E.coli undecaprenyl pyrophosphate synthase'''
+
===Structure of E.coli undecaprenyl pyrophosphate synthase===
-
==Overview==
+
<!--
-
The Escherichia coli undecaprayl-pyrophosphate synthase (UPPs) structure has been solved using the single wavelength anomalous diffraction method. The putative substrate-binding site is located near the end of the betaA-strand with Asp-26 playing a critical catalytic role. In both subunits, an elongated hydrophobic tunnel is found, surrounded by four beta-strands (betaA-betaB-betaD-betaC) and two helices (alpha2 and alpha3) and lined at the bottom with large residues Ile-62, Leu-137, Val-105, and His-103. The product distributions formed by the use of the I62A, V105A, and H103A mutants are similar to those observed for wild-type UPPs. Catalysis by the L137A UPPs, on the other hand, results in predominantly the formation of the C(70) polymer rather than the C(55) polymer. Ala-69 and Ala-143 are located near the top of the tunnel. In contrast to the A143V reaction, the C(30) intermediate is formed to a greater extent and is longer lived in the process catalyzed by the A69L mutant. These findings suggest that the small side chain of Ala-69 is required for rapid elongation to the C(55) product, whereas the large hydrophobic side chain of Leu-137 is required to limit the elongation to the C(55) product. The roles of residues located on a flexible loop were investigated. The S71A, N74A, or R77A mutants displayed 25-200-fold decrease in k(cat) values. W75A showed an 8-fold increase of the FPP K(m) value, and 22-33-fold increases in the IPP K(m) values were observed for E81A and S71A. The loop may function to bridge the interaction of IPP with FPP, needed to initiate the condensation reaction and serve as a hinge to control the substrate binding and product release.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11581264}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11581264 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11581264}}
==About this Structure==
==About this Structure==
Line 35: Line 39:
[[Category: Product chain length]]
[[Category: Product chain length]]
[[Category: Rossmann fold]]
[[Category: Rossmann fold]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:32:05 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:34:49 2008''

Revision as of 17:34, 1 July 2008

Image:1jp3.png

Template:STRUCTURE 1jp3

Structure of E.coli undecaprenyl pyrophosphate synthase

Template:ABSTRACT PUBMED 11581264

About this Structure

1JP3 is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Mechanism of product chain length determination and the role of a flexible loop in Escherichia coli undecaprenyl-pyrophosphate synthase catalysis., Ko TP, Chen YK, Robinson H, Tsai PC, Gao YG, Chen AP, Wang AH, Liang PH, J Biol Chem. 2001 Dec 14;276(50):47474-82. Epub 2001 Oct 1. PMID:11581264

Page seeded by OCA on Tue Jul 1 20:34:49 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jp3"
Personal tools