2ltn

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2ltn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ltn, resolution 1.7&Aring;" /> '''DESIGN, EXPRESSION, A...)
Line 1: Line 1:
-
[[Image:2ltn.jpg|left|200px]]<br /><applet load="2ltn" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2ltn.jpg|left|200px]]<br /><applet load="2ltn" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ltn, resolution 1.7&Aring;" />
caption="2ltn, resolution 1.7&Aring;" />
'''DESIGN, EXPRESSION, AND CRYSTALLIZATION OF RECOMBINANT LECTIN FROM THE GARDEN PEA (PISUM SATIVUM)'''<br />
'''DESIGN, EXPRESSION, AND CRYSTALLIZATION OF RECOMBINANT LECTIN FROM THE GARDEN PEA (PISUM SATIVUM)'''<br />
==Overview==
==Overview==
-
The propeptide form of the lectin from the garden pea (Pisum sativum, agglutinin) has been expressed in Escherichia coli by attaching its cDNA, to an inducible promoter. By a number of criteria, including the ability, to form dimers, hemagglutination titer, Western blot, and enzyme-linked, immunosorbent assay, the resulting propeptide molecule is virtually, indistinguishable from the mature proteolytically processed lectin, isolated from peas. Preliminary crystallization experiments using the, recombinant propeptide lectin yield crystals in space group P2(1)2(1)2(1), with a = 64.8 A, b = 73.8 A, and c = 109.0 A (1 A = 0.1 nm) that diffract, to 2.8-A resolution. This unit cell size is quite similar to the unit cell, determined for native pea lectin, suggesting that the overall structure of, the recombinant prolectin is virtually identical.
+
The propeptide form of the lectin from the garden pea (Pisum sativum agglutinin) has been expressed in Escherichia coli by attaching its cDNA to an inducible promoter. By a number of criteria, including the ability to form dimers, hemagglutination titer, Western blot, and enzyme-linked immunosorbent assay, the resulting propeptide molecule is virtually indistinguishable from the mature proteolytically processed lectin isolated from peas. Preliminary crystallization experiments using the recombinant propeptide lectin yield crystals in space group P2(1)2(1)2(1) with a = 64.8 A, b = 73.8 A, and c = 109.0 A (1 A = 0.1 nm) that diffract to 2.8-A resolution. This unit cell size is quite similar to the unit cell determined for native pea lectin, suggesting that the overall structure of the recombinant prolectin is virtually identical.
==About this Structure==
==About this Structure==
-
2LTN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with MN and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2LTN OCA].
+
2LTN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Pisum_sativum Pisum sativum] with <scene name='pdbligand=MN:'>MN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LTN OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Einspahr, H.]]
[[Category: Einspahr, H.]]
-
[[Category: Phillips, S.R.]]
+
[[Category: Phillips, S R.]]
-
[[Category: Suddath, F.L.]]
+
[[Category: Suddath, F L.]]
[[Category: CA]]
[[Category: CA]]
[[Category: MN]]
[[Category: MN]]
[[Category: lectin]]
[[Category: lectin]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:42:30 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:07:15 2008''

Revision as of 16:07, 21 February 2008

Image:2ltn.jpg

2ltn, resolution 1.7Å

Drag the structure with the mouse to rotate

DESIGN, EXPRESSION, AND CRYSTALLIZATION OF RECOMBINANT LECTIN FROM THE GARDEN PEA (PISUM SATIVUM)

Overview

The propeptide form of the lectin from the garden pea (Pisum sativum agglutinin) has been expressed in Escherichia coli by attaching its cDNA to an inducible promoter. By a number of criteria, including the ability to form dimers, hemagglutination titer, Western blot, and enzyme-linked immunosorbent assay, the resulting propeptide molecule is virtually indistinguishable from the mature proteolytically processed lectin isolated from peas. Preliminary crystallization experiments using the recombinant propeptide lectin yield crystals in space group P2(1)2(1)2(1) with a = 64.8 A, b = 73.8 A, and c = 109.0 A (1 A = 0.1 nm) that diffract to 2.8-A resolution. This unit cell size is quite similar to the unit cell determined for native pea lectin, suggesting that the overall structure of the recombinant prolectin is virtually identical.

About this Structure

2LTN is a Protein complex structure of sequences from Pisum sativum with and as ligands. Full crystallographic information is available from OCA.

Reference

Design, expression, and crystallization of recombinant lectin from the garden pea (Pisum sativum)., Prasthofer T, Phillips SR, Suddath FL, Engler JA, J Biol Chem. 1989 Apr 25;264(12):6793-6. PMID:2708344

Page seeded by OCA on Thu Feb 21 18:07:15 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ltn"
Personal tools