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.


2h6h

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2h6h.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2h6h.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2h6h| PDB=2h6h | SCENE= }}
{{STRUCTURE_2h6h| PDB=2h6h | SCENE= }}
-
'''Y365F Protein Farnesyltransferase Mutant Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.8A'''
+
===Y365F Protein Farnesyltransferase Mutant Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.8A===
-
==Overview==
+
<!--
-
Posttranslational modifications are essential for the proper function of a number of proteins in the cell. One such modification, the covalent attachment of a single isoprenoid lipid (prenylation), is carried out by the CaaX prenyltransferases, protein farnesyltransferase (FTase) and protein geranylgeranyltransferase type-I (GGTase-I). Substrate proteins of these two enzymes are involved in a variety of cellular functions but are largely associated with signal transduction. These modified proteins include members of the Ras superfamily, heterotrimeric G-proteins, centromeric proteins, and a number of proteins involved in nuclear integrity. Although FTase and GGTase-I are highly homologous, they are quite selective for their substrates, particularly for their isoprenoid diphosphate substrates, FPP and GGPP, respectively. Here, we present both crystallographic and kinetic analyses of mutants designed to explore this isoprenoid specificity and demonstrate that this specificity is dependent upon two enzyme residues in the beta subunits of the enzymes, W102beta and Y365beta in FTase (T49beta and F324beta, respectively, in GGTase-I).
+
The line below this paragraph, {{ABSTRACT_PUBMED_16893176}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 16893176 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_16893176}}
==About this Structure==
==About this Structure==
Line 34: Line 38:
[[Category: Ra]]
[[Category: Ra]]
[[Category: Substrate selectivity]]
[[Category: Substrate selectivity]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:55:22 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 13:16:10 2008''

Revision as of 10:16, 27 July 2008

Image:2h6h.png

Template:STRUCTURE 2h6h

Y365F Protein Farnesyltransferase Mutant Complexed with a Farnesylated DDPTASACVLS Peptide Product at 1.8A

Template:ABSTRACT PUBMED 16893176

About this Structure

2H6H is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Conversion of protein farnesyltransferase to a geranylgeranyltransferase., Terry KL, Casey PJ, Beese LS, Biochemistry. 2006 Aug 15;45(32):9746-55. PMID:16893176

Page seeded by OCA on Sun Jul 27 13:16:10 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2h6h"
Personal tools