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.


1fj2

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1fj2.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1fj2.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1fj2| PDB=1fj2 | SCENE= }}
{{STRUCTURE_1fj2| PDB=1fj2 | SCENE= }}
-
'''Crystal structure of the human acyl protein thioesterase 1 at 1.5 A resolution'''
+
===Crystal structure of the human acyl protein thioesterase 1 at 1.5 A resolution===
-
==Overview==
+
<!--
-
BACKGROUND: Many proteins undergo posttranslational modifications involving covalent attachment of lipid groups. Among them is palmitoylation, a dynamic, reversible process that affects trimeric G proteins and Ras and constitutes a regulatory mechanism for signal transduction pathways. Recently, an acylhydrolase previously identified as lysophospholipase has been shown to function as an acyl protein thioesterase, which catalyzes depalmitoylation of Galpha proteins as well as Ras. Its amino acid sequence suggested that the protein is evolutionarily related to neutral lipases and other thioesterases, but direct structural information was not available. RESULTS: We have solved the crystal structure of the human putative Galpha-regulatory protein acyl thioesterase (hAPT1) with a single data set collected from a crystal containing the wild-type protein. The phases were calculated to 1.8 A resolution based on anomalous scattering from Br(-) ions introduced in the cryoprotectant solution in which the crystal was soaked for 20 s. The model was refined against data extending to a resolution of 1.5 A to an R factor of 18.6%. The enzyme is a member of the ubiquitous alpha/beta hydrolase family, which includes other acylhydrolases such as the palmitoyl protein thioesterase (PPT1). CONCLUSIONS: The human APT1 is closely related to a previously described carboxylesterase from Pseudomonas fluorescens. The active site contains a catalytic triad of Ser-114, His-203, and Asp-169. Like carboxylesterase, hAPT1 appears to be dimeric, although the mutual disposition of molecules in the two dimers differs. Unlike carboxylesterase, the substrate binding pocket and the active site of hAPT1 are occluded by the dimer interface, suggesting that the enzyme must dissociate upon interaction with substrate.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11080636}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11080636 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11080636}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Sad]]
[[Category: Sad]]
[[Category: Serine hydrolase]]
[[Category: Serine hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:23:14 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 03:20:50 2008''

Revision as of 00:20, 1 July 2008

Image:1fj2.png

Template:STRUCTURE 1fj2

Crystal structure of the human acyl protein thioesterase 1 at 1.5 A resolution

Template:ABSTRACT PUBMED 11080636

About this Structure

1FJ2 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A., Devedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS, Structure. 2000 Nov 15;8(11):1137-46. PMID:11080636

Page seeded by OCA on Tue Jul 1 03:20:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fj2"
Personal tools