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.


1kuv

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1kuv.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1kuv.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1kuv| PDB=1kuv | SCENE= }}
{{STRUCTURE_1kuv| PDB=1kuv | SCENE= }}
-
'''X-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition'''
+
===X-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition===
-
==Overview==
+
<!--
-
The structure of serotonin N-acetyltransferase (also known as arylalkylamine N-acetyltransferase; AANAT) bound to a potent bisubstrate analog inhibitor has been determined at 2.0 A resolution using a two-edge (Se, Br) multiwavelength anomalous diffraction (MAD) experiment. This acetyl-CoA dependent enzyme is a member of the GCN5-related family of N-acetyltransferases (GNATs), which share four conserved sequence motifs (A-D). In serotonin N-acetyltransferase, motif A adopts an alpha/beta conformation characteristic of the phylogenetically invariant cofactor binding site seen in all previously characterized GNATs. Motif B displays a significantly lower level of conservation among family members, giving rise to a novel alpha/beta structure for the serotonin binding slot. Utilization of a brominated CoA-S-acetyl-tryptamine-bisubstrate analog inhibitor and the MAD method permitted conclusive identification of two radically different conformations for the tryptamine moiety in the catalytic site (cis and trans). A second high-resolution X-ray structure of the enzyme bound to a bisubstrate analog inhibitor, with a longer tether between the acetyl-CoA and tryptamine moieties, demonstrates only the trans conformation. Given a previous proposal that AANAT can catalyze an alkyltransferase reaction in a conformationally altered active site relative to its acetyltransferase activity, it is possible that the two conformations of the bisubstrate analog observed crystallographically correspond to these alternative reaction pathways. Our findings may ultimately lead to the design of analogs with improved AANAT inhibitory properties for in vivo applications.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11902838}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11902838 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11902838}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Bisubstrate analog]]
[[Category: Bisubstrate analog]]
[[Category: Enzyme-inhibitor complex]]
[[Category: Enzyme-inhibitor complex]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:11:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:02:43 2008''

Revision as of 08:02, 2 July 2008

Image:1kuv.png

Template:STRUCTURE 1kuv

X-ray Crystallographic Studies of Serotonin N-acetyltransferase Catalysis and Inhibition

Template:ABSTRACT PUBMED 11902838

About this Structure

1KUV is a Single protein structure of sequence from Ovis aries. Full crystallographic information is available from OCA.

Reference

X-ray crystallographic studies of serotonin N-acetyltransferase catalysis and inhibition., Wolf E, De Angelis J, Khalil EM, Cole PA, Burley SK, J Mol Biol. 2002 Mar 22;317(2):215-24. PMID:11902838

Page seeded by OCA on Wed Jul 2 11:02:43 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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