We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2ree

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2ree.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2ree.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ree| PDB=2ree | SCENE= }}
{{STRUCTURE_2ree| PDB=2ree | SCENE= }}
-
'''Crystal structure of the loading GNATL domain of CurA from Lyngbya majuscula'''
+
===Crystal structure of the loading GNATL domain of CurA from Lyngbya majuscula===
-
==Overview==
+
<!--
-
An unexpected biochemical strategy for chain initiation is described for the loading module of the polyketide synthase of curacin A, an anticancer lead derived from the marine cyanobacterium Lyngbya majuscula. A central GCN5-related N-acetyltransferase (GNAT) domain bears bifunctional decarboxylase/S-acetyltransferase activity, both unprecedented for the GNAT superfamily. A CurA loading tridomain, consisting of an adaptor domain, the GNAT domain, and an acyl carrier protein, was assessed biochemically, revealing that a domain showing homology to GNAT (GNAT(L)) catalyzes (i) decarboxylation of malonyl-coenzyme A (malonyl-CoA) to acetyl-CoA and (ii) direct S-acetyl transfer from acetyl-CoA to load an adjacent acyl carrier protein domain (ACP(L)). Moreover, the N-terminal adapter domain was shown to facilitate acetyl-group transfer. Crystal structures of GNAT(L) were solved at 1.95 angstroms (ligand-free form) and 2.75 angstroms (acyl-CoA complex), showing distinct substrate tunnels for acyl-CoA and holo-ACP(L) binding. Modeling and site-directed mutagenesis experiments demonstrated that histidine-389 and threonine-355, at the convergence of the CoA and ACP tunnels, participate in malonyl-CoA decarboxylation but not in acetyl-group transfer. Decarboxylation precedes acetyl-group transfer, leading to acetyl-ACP(L) as the key curacin A starter unit.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17991863}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17991863 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17991863}}
==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: S-acetyltransferase]]
[[Category: S-acetyltransferase]]
[[Category: Transferase]]
[[Category: Transferase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 16:44:37 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 03:25:41 2008''

Revision as of 00:25, 28 July 2008

Image:2ree.png

Template:STRUCTURE 2ree

Crystal structure of the loading GNATL domain of CurA from Lyngbya majuscula

Template:ABSTRACT PUBMED 17991863

About this Structure

2REE is a Single protein structure of sequence from Lyngbya majuscula. Full crystallographic information is available from OCA.

Reference

GNAT-like strategy for polyketide chain initiation., Gu L, Geders TW, Wang B, Gerwick WH, Hakansson K, Smith JL, Sherman DH, Science. 2007 Nov 9;318(5852):970-4. PMID:17991863

Page seeded by OCA on Mon Jul 28 03:25:41 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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