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.

1du4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1du4.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1du4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1du4| PDB=1du4 | SCENE= }}
{{STRUCTURE_1du4| PDB=1du4 | SCENE= }}
-
'''THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE OTHER STRUCTURE DETAILS'''
+
===THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE OTHER STRUCTURE DETAILS===
-
==Overview==
+
<!--
-
The already known X-ray structures of lipases provide little evidence about initial, discrete structural steps occurring in the first phases of their activation in the presence of lipids (process referred to as interfacial activation). To address this problem, five new Thermomyces (formerly Humicola) lanuginosa lipase (TlL) crystal structures have been solved and compared with four previously reported structures of this enzyme. The bias coming from different crystallization media has been minimized by the growth of all crystals under the same crystallization conditions, in the presence of detergent/lipid analogues, with low or high ionic strength as the only main variable. Resulting structures and their characteristic features allowed the identification of three structurally distinct species of this enzyme: low activity form (LA), activated form (A), and fully Active (FA) form. The isomerization of the Cys268-Cys22 disulfide, synchronized with the formation of a new, short alpha(0) helix and flipping of the Arg84 (Arginine switch) located in the lid's proximal hinge, have been postulated as the key, structural factors of the initial transitions between LA and A forms. The experimental results were supplemented by theoretical calculations. The magnitude of the activation barrier between LA (ground state) and A (end state) forms of TlL (10.6 kcal/mol) is comparable to the enthalpic barriers typical for ring flips and disulfide isomerizations at ambient temperatures. This suggests that the sequence of the structural changes, as exemplified in various TlL crystal structures, mirror those that may occur during interfacial activation.
+
The line below this paragraph, {{ABSTRACT_PUBMED_11106485}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 11106485 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_11106485}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Lipase]]
[[Category: Lipase]]
[[Category: Thermomyces linuginosa]]
[[Category: Thermomyces linuginosa]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:16:40 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 23:37:13 2008''

Revision as of 20:37, 30 June 2008

Image:1du4.png

Template:STRUCTURE 1du4

THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE OTHER STRUCTURE DETAILS

Template:ABSTRACT PUBMED 11106485

About this Structure

1DU4 is a Single protein structure of sequence from Thermomyces lanuginosus. Full crystallographic information is available from OCA.

Reference

Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase., Brzozowski AM, Savage H, Verma CS, Turkenburg JP, Lawson DM, Svendsen A, Patkar S, Biochemistry. 2000 Dec 12;39(49):15071-82. PMID:11106485

Page seeded by OCA on Mon Jun 30 23:37:13 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1du4"
Personal tools