2es4

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(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...)
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[[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==
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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.
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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==
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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].
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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==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Triacylglycerol lipase]]
[[Category: Triacylglycerol lipase]]
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[[Category: Gelder, P.Van.]]
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[[Category: Gelder, P Van.]]
[[Category: Pauwels, K.]]
[[Category: Pauwels, K.]]
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[[Category: Savvides, S.N.]]
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[[Category: Savvides, S N.]]
[[Category: Tommassen, J.]]
[[Category: Tommassen, J.]]
[[Category: Wyns, L.]]
[[Category: Wyns, L.]]
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[[Category: triacylglycerol hydrolase]]
[[Category: triacylglycerol hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:06:49 2007''
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''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

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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

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