1pz4
From Proteopedia
(New page: 200px<br /><applet load="1pz4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pz4, resolution 1.35Å" /> '''The structural deter...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1pz4.jpg|left|200px]]<br /><applet load="1pz4" size=" | + | [[Image:1pz4.jpg|left|200px]]<br /><applet load="1pz4" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1pz4, resolution 1.35Å" /> | caption="1pz4, resolution 1.35Å" /> | ||
'''The structural determination of an insect (mosquito) Sterol Carrier Protein-2 with a ligand bound C16 Fatty Acid at 1.35 A resolution'''<br /> | '''The structural determination of an insect (mosquito) Sterol Carrier Protein-2 with a ligand bound C16 Fatty Acid at 1.35 A resolution'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Yellow fever mosquito sterol carrier protein (SCP-2) is known to bind to | + | Yellow fever mosquito sterol carrier protein (SCP-2) is known to bind to cholesterol. We report here the three-dimensional structure of the complex of SCP-2 from Aedes aegypti with a C16 fatty acid to 1.35-A resolution. The protein fold is exceedingly similar to the human and rabbit proteins, which consist of a five-stranded beta-sheet that exhibits strand order 3-2-1-4-5 with an accompanying layer of four alpha-helices that cover the beta-sheet. A large cavity exists at the interface of the layer alpha-helices and the beta-sheet, which serves as the fatty acid binding site. The carboxylate moiety of the fatty acid is coordinated by a short loop that connects the first alpha-helix to the first beta-strand, whereas the acyl chain extends deep into the interior of the protein. Interestingly, the orientation of the fatty acid is opposite to the observed orientation for Triton X-100 in the SCP-2-like domain from the peroxisomal multifunctional enzyme (Haapalainen, A. M., van Aalten, D. M., Merilainen, G., Jalonen, J. E., Pirila, P., Wierenga, R. K., Hiltunen, J. K., and Glumoff, T. (2001) J. Mol. Biol. 313, 1127-1138). The present study suggests that the binding pocket in the SCP-2 family of proteins may exhibit conformational flexibility to allow coordination of a variety of lipids. |
==About this Structure== | ==About this Structure== | ||
| - | 1PZ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aedes_aegypti Aedes aegypti] with PLM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1PZ4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aedes_aegypti Aedes aegypti] with <scene name='pdbligand=PLM:'>PLM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PZ4 OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Aedes aegypti]] | [[Category: Aedes aegypti]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Dyer, D | + | [[Category: Dyer, D H.]] |
| - | [[Category: Holden, H | + | [[Category: Holden, H M.]] |
[[Category: Lan, Q.]] | [[Category: Lan, Q.]] | ||
[[Category: Lovell, S.]] | [[Category: Lovell, S.]] | ||
[[Category: Rayment, I.]] | [[Category: Rayment, I.]] | ||
| - | [[Category: Thoden, J | + | [[Category: Thoden, J B.]] |
[[Category: PLM]] | [[Category: PLM]] | ||
[[Category: alpha and beta]] | [[Category: alpha and beta]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:08 2008'' |
Revision as of 12:34, 21 February 2008
|
The structural determination of an insect (mosquito) Sterol Carrier Protein-2 with a ligand bound C16 Fatty Acid at 1.35 A resolution
Overview
Yellow fever mosquito sterol carrier protein (SCP-2) is known to bind to cholesterol. We report here the three-dimensional structure of the complex of SCP-2 from Aedes aegypti with a C16 fatty acid to 1.35-A resolution. The protein fold is exceedingly similar to the human and rabbit proteins, which consist of a five-stranded beta-sheet that exhibits strand order 3-2-1-4-5 with an accompanying layer of four alpha-helices that cover the beta-sheet. A large cavity exists at the interface of the layer alpha-helices and the beta-sheet, which serves as the fatty acid binding site. The carboxylate moiety of the fatty acid is coordinated by a short loop that connects the first alpha-helix to the first beta-strand, whereas the acyl chain extends deep into the interior of the protein. Interestingly, the orientation of the fatty acid is opposite to the observed orientation for Triton X-100 in the SCP-2-like domain from the peroxisomal multifunctional enzyme (Haapalainen, A. M., van Aalten, D. M., Merilainen, G., Jalonen, J. E., Pirila, P., Wierenga, R. K., Hiltunen, J. K., and Glumoff, T. (2001) J. Mol. Biol. 313, 1127-1138). The present study suggests that the binding pocket in the SCP-2 family of proteins may exhibit conformational flexibility to allow coordination of a variety of lipids.
About this Structure
1PZ4 is a Single protein structure of sequence from Aedes aegypti with as ligand. Full crystallographic information is available from OCA.
Reference
The structural determination of an insect sterol carrier protein-2 with a ligand-bound C16 fatty acid at 1.35-A resolution., Dyer DH, Lovell S, Thoden JB, Holden HM, Rayment I, Lan Q, J Biol Chem. 2003 Oct 3;278(40):39085-91. Epub 2003 Jul 10. PMID:12855689
Page seeded by OCA on Thu Feb 21 14:34:08 2008
Categories: Aedes aegypti | Single protein | Dyer, D H. | Holden, H M. | Lan, Q. | Lovell, S. | Rayment, I. | Thoden, J B. | PLM | Alpha and beta
