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.

1ult

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1ult.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1ult.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1ult| PDB=1ult | SCENE= }}
{{STRUCTURE_1ult| PDB=1ult | SCENE= }}
-
'''Crystal structure of tt0168 from Thermus thermophilus HB8'''
+
===Crystal structure of tt0168 from Thermus thermophilus HB8===
-
==Overview==
+
<!--
-
Long chain fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of long chain fatty acyl-CoA esters. We report the first crystal structures of long chain fatty acyl-CoA synthetase homodimer (LC-FACS) from Thermus thermophilus HB8 (ttLC-FACS), including complexes with the ATP analogue adenosine 5'-(beta,gamma-imido) triphosphate (AMP-PNP) and myristoyl-AMP. ttLC-FACS is a member of the adenylate forming enzyme superfamily that catalyzes the ATP-dependent acylation of fatty acid in a two-step reaction. The first reaction step was shown to propagate in AMP-PNP complex crystals soaked with myristate solution. Myristoyl-AMP was identified as the intermediate. The AMP-PNP and the myristoyl-AMP complex structures show an identical closed conformation of the small C-terminal domains, whereas the uncomplexed form shows a variety of open conformations. Upon ATP binding, the fatty acid-binding tunnel gated by an aromatic residue opens to the ATP-binding site. The gated fatty acid-binding tunnel appears only to allow one-way movement of the fatty acid during overall catalysis. The protein incorporates a hydrophobic branch from the fatty acid-binding tunnel that is responsible for substrate specificity. Based on these high resolution crystal structures, we propose a unidirectional Bi Uni Uni Bi Ping-Pong mechanism for the two-step acylation by ttLC-FACS.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15145952}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15145952 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15145952}}
==About this Structure==
==About this Structure==
Line 41: Line 45:
[[Category: Rsgi]]
[[Category: Rsgi]]
[[Category: Structural genomic]]
[[Category: Structural genomic]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 11:24:09 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 07:46:50 2008''

Revision as of 04:46, 29 July 2008

Image:1ult.png

Template:STRUCTURE 1ult

Crystal structure of tt0168 from Thermus thermophilus HB8

Template:ABSTRACT PUBMED 15145952

About this Structure

1ULT is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.

Reference

Structural basis of the substrate-specific two-step catalysis of long chain fatty acyl-CoA synthetase dimer., Hisanaga Y, Ago H, Nakagawa N, Hamada K, Ida K, Yamamoto M, Hori T, Arii Y, Sugahara M, Kuramitsu S, Yokoyama S, Miyano M, J Biol Chem. 2004 Jul 23;279(30):31717-26. Epub 2004 May 15. PMID:15145952

Page seeded by OCA on Tue Jul 29 07:46:50 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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