1kcm: Difference between revisions

Revision as of 14:32, 21 February 2008

Crystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms Resolution

OverviewOverview

Phosphatidylinositol transfer protein alpha (PITP alpha) is a ubiquitous and highly conserved protein in multicellular eukaryotes that catalyzes the exchange of phospholipids between membranes in vitro and participates in cellular phospholipid metabolism, signal transduction and vesicular trafficking in vivo. Here we report the three-dimensional crystal structure of a phospholipid-free mouse PITP alpha at 2.0 A resolution. The structure reveals an open conformation characterized by a channel running through the protein. The channel is created by opening the phospholipid-binding cavity on one side by displacement of the C-terminal region and a hydrophobic lipid exchange loop, and on the other side by flattening of the central beta-sheet. The relaxed conformation is stabilized at the proposed membrane association site by hydrophobic interactions with a crystallographically related molecule, creating an intimate dimer. The observed open conformer is consistent with a membrane-bound state of PITP and suggests a mechanism for membrane anchoring and the presentation of phosphatidylinositol to kinases and phospholipases after its extraction from the membrane. Coordinates have been deposited in the Protein Data Bank (accession No. 1KCM).

About this StructureAbout this Structure

1KCM is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Structure of apo-phosphatidylinositol transfer protein alpha provides insight into membrane association., Schouten A, Agianian B, Westerman J, Kroon J, Wirtz KW, Gros P, EMBO J. 2002 May 1;21(9):2117-21. PMID:11980708

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OCA

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 '''Crystal Structure of Mouse PITP Alpha Void of Bound Phospholipid at 2.0 Angstroms Resolution'''<br />
 ==Overview==
-Phosphatidylinositol transfer protein alpha (PITP alpha) is a ubiquitous, and highly conserved protein in multicellular eukaryotes that catalyzes, the exchange of phospholipids between membranes in vitro and participates, in cellular phospholipid metabolism, signal transduction and vesicular, trafficking in vivo. Here we report the three-dimensional crystal, structure of a phospholipid-free mouse PITP alpha at 2.0 A resolution. The, structure reveals an open conformation characterized by a channel running, through the protein. The channel is created by opening the, phospholipid-binding cavity on one side by displacement of the C-terminal, region and a hydrophobic lipid exchange loop, and on the other side by, flattening of the central beta-sheet. The relaxed conformation is, stabilized at the proposed membrane association site by hydrophobic, interactions with a crystallographically related molecule, creating an, intimate dimer. The observed open conformer is consistent with a, membrane-bound state of PITP and suggests a mechanism for membrane, anchoring and the presentation of phosphatidylinositol to kinases and, phospholipases after its extraction from the membrane. Coordinates have, been deposited in the Protein Data Bank (accession No. 1KCM).
+Phosphatidylinositol transfer protein alpha (PITP alpha) is a ubiquitous and highly conserved protein in multicellular eukaryotes that catalyzes the exchange of phospholipids between membranes in vitro and participates in cellular phospholipid metabolism, signal transduction and vesicular trafficking in vivo. Here we report the three-dimensional crystal structure of a phospholipid-free mouse PITP alpha at 2.0 A resolution. The structure reveals an open conformation characterized by a channel running through the protein. The channel is created by opening the phospholipid-binding cavity on one side by displacement of the C-terminal region and a hydrophobic lipid exchange loop, and on the other side by flattening of the central beta-sheet. The relaxed conformation is stabilized at the proposed membrane association site by hydrophobic interactions with a crystallographically related molecule, creating an intimate dimer. The observed open conformer is consistent with a membrane-bound state of PITP and suggests a mechanism for membrane anchoring and the presentation of phosphatidylinositol to kinases and phospholipases after its extraction from the membrane. Coordinates have been deposited in the Protein Data Bank (accession No. 1KCM).
 ==About this Structure==
-KCM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KCM OCA].
+KCM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KCM OCA].
 ==Reference==
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 [[Category: Schouten, A.]]
 [[Category: Westerman, J.]]
-[[Category: Wirtz, K.W.A.]]
+[[Category: Wirtz, K W.A.]]
 [[Category: phospholipid binding protein]]
 [[Category: phospholipid transport]]
 [[Category: pitp]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:03:49 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:32:33 2008''