1ein: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 1: Line 1:
[[Image:1ein.gif|left|200px]]<br /><applet load="1ein" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1ein.gif|left|200px]]
caption="1ein, resolution 3.0&Aring;" />
 
'''THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE'''<br />
{{Structure
|PDB= 1ein |SIZE=350|CAPTION= <scene name='initialview01'>1ein</scene>, resolution 3.0&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=PLC:DIUNDECYL PHOSPHATIDYL CHOLINE'>PLC</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3]
|GENE=
}}
 
'''THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE'''
 


==Overview==
==Overview==
Line 7: Line 16:


==About this Structure==
==About this Structure==
1EIN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermomyces_lanuginosus Thermomyces lanuginosus] with <scene name='pdbligand=PLC:'>PLC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Triacylglycerol_lipase Triacylglycerol lipase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.1.3 3.1.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EIN OCA].  
1EIN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermomyces_lanuginosus Thermomyces lanuginosus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EIN OCA].  


==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11106485 11106485]
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:[http://www.ncbi.nlm.nih.gov/pubmed/11106485 11106485]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Thermomyces lanuginosus]]
[[Category: Thermomyces lanuginosus]]
Line 19: Line 28:
[[Category: alpha-beta structure]]
[[Category: alpha-beta structure]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:28:07 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:56:08 2008''

Revision as of 11:56, 20 March 2008

File:1ein.gif


PDB ID 1ein

Drag the structure with the mouse to rotate
, resolution 3.0Å
Ligands:
Activity: Triacylglycerol lipase, with EC number 3.1.1.3
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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.

About this StructureAbout this Structure

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

ReferenceReference

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 Thu Mar 20 10:56:08 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA