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.

1u8u

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1u8u.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1u8u.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1u8u| PDB=1u8u | SCENE= }}
{{STRUCTURE_1u8u| PDB=1u8u | SCENE= }}
-
'''E. coli Thioesterase I/Protease I/Lysophospholiase L1 in complexed with octanoic acid'''
+
===E. coli Thioesterase I/Protease I/Lysophospholiase L1 in complexed with octanoic acid===
-
==Overview==
+
<!--
-
Escherichia coli thioesterase I/protease I/lysophospholipase L(1) (TAP) is a multifunctional lysophospholipase and acyl-CoA thioesterase with a SGNH-hydrolase fold. The relationship between TAP's structure and its versatile substrate specificity, however, is unclear. Here, we present the crystal structure of TAP in complex with octanoic acid (TAP-OCA; OCA, a free fatty acid with eight carbon atoms, C(8)). A structural comparison of native TAP with TAP-OCA reveals a remarkable conformational change in loop(75)(-)(80), called "switch loop movement", upon OCA binding to the substrate-binding crevice of TAP. OCA binding to the substrate-binding crevice results in a continuous hydrophobic surface, which triggers switch loop movement. The switch loop movement is acyl chain length dependent, with an effect of stabilizing the Michaelis complex (MC) of TAP during catalysis, and is essential for TAP's substrate preference. The finding of a sulfate ion binding site in the TAP structures, together with previous enzyme kinetic analyses, leads us to postulate that a putative CoA binding site is essential for efficient catalysis of thioesters in TAP. We also present the crystal structure of L109P-OCA (TAP's L109P mutant in complex with OCA), in which Leu109 mutated to Pro109 abolishes switch loop movement. This result strengthens our hypothesis that the switch loop movement is induced by hydrophobic interactions.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15697222}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15697222 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15697222}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Protease]]
[[Category: Protease]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:54:33 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:01:19 2008''

Revision as of 10:01, 29 July 2008

Image:1u8u.png

Template:STRUCTURE 1u8u

E. coli Thioesterase I/Protease I/Lysophospholiase L1 in complexed with octanoic acid

Template:ABSTRACT PUBMED 15697222

About this Structure

1U8U is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Substrate specificities of Escherichia coli thioesterase I/protease I/lysophospholipase L1 are governed by its switch loop movement., Lo YC, Lin SC, Shaw JF, Liaw YC, Biochemistry. 2005 Feb 15;44(6):1971-9. PMID:15697222

Page seeded by OCA on Tue Jul 29 13:01:19 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1u8u"
Personal tools