This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2es4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2es4" size="450" color="white" frame="true" align="right" spinBox="true" caption="2es4, resolution 1.85&Aring;" /> '''Crystal structure of...)
Line 1: Line 1:
-
[[Image:2es4.gif|left|200px]]<br /><applet load="2es4" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2es4.gif|left|200px]]<br /><applet load="2es4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2es4, resolution 1.85&Aring;" />
caption="2es4, resolution 1.85&Aring;" />
'''Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase'''<br />
'''Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase'''<br />
==Overview==
==Overview==
-
Secretion via the type II secretion pathway in Gram-negative bacteria, often relies crucially on steric chaperones in the periplasm. Here, we, report the crystal structure of the soluble form of a lipase-specific, foldase (Lif) from Burkholderia glumae in complex with its cognate lipase., The structure reveals how Lif uses a novel alpha-helical scaffold to, embrace lipase, thereby creating an unusually extensive folding platform.
+
Secretion via the type II secretion pathway in Gram-negative bacteria often relies crucially on steric chaperones in the periplasm. Here, we report the crystal structure of the soluble form of a lipase-specific foldase (Lif) from Burkholderia glumae in complex with its cognate lipase. The structure reveals how Lif uses a novel alpha-helical scaffold to embrace lipase, thereby creating an unusually extensive folding platform.
==About this Structure==
==About this Structure==
-
2ES4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Burkholderia_glumae Burkholderia glumae] with CA and IOD as [http://en.wikipedia.org/wiki/ligands ligands]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2ES4 OCA].
+
2ES4 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Burkholderia_glumae Burkholderia glumae] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=IOD:'>IOD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. 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=2ES4 OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Triacylglycerol lipase]]
[[Category: Triacylglycerol lipase]]
-
[[Category: Gelder, P.Van.]]
+
[[Category: Gelder, P Van.]]
[[Category: Pauwels, K.]]
[[Category: Pauwels, K.]]
-
[[Category: Savvides, S.N.]]
+
[[Category: Savvides, S N.]]
[[Category: Tommassen, J.]]
[[Category: Tommassen, J.]]
[[Category: Wyns, L.]]
[[Category: Wyns, L.]]
Line 28: Line 28:
[[Category: triacylglycerol hydrolase]]
[[Category: triacylglycerol hydrolase]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:06:49 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:14:02 2008''

Revision as of 15:14, 21 February 2008


2es4, resolution 1.85Å

Drag the structure with the mouse to rotate

Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase

Overview

Secretion via the type II secretion pathway in Gram-negative bacteria often relies crucially on steric chaperones in the periplasm. Here, we report the crystal structure of the soluble form of a lipase-specific foldase (Lif) from Burkholderia glumae in complex with its cognate lipase. The structure reveals how Lif uses a novel alpha-helical scaffold to embrace lipase, thereby creating an unusually extensive folding platform.

About this Structure

2ES4 is a Protein complex structure of sequences from Burkholderia glumae with and as ligands. Active as Triacylglycerol lipase, with EC number 3.1.1.3 Full crystallographic information is available from OCA.

Reference

Structure of a membrane-based steric chaperone in complex with its lipase substrate., Pauwels K, Lustig A, Wyns L, Tommassen J, Savvides SN, Van Gelder P, Nat Struct Mol Biol. 2006 Apr;13(4):374-5. Epub 2006 Mar 5. PMID:16518399

Page seeded by OCA on Thu Feb 21 17:14:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools