2ext

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="2ext" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ext, resolution 1.80&Aring;" /> '''TRAP4 (engineered TR...)
Line 1: Line 1:
-
[[Image:2ext.gif|left|200px]]<br /><applet load="2ext" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:2ext.gif|left|200px]]<br /><applet load="2ext" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ext, resolution 1.80&Aring;" />
caption="2ext, resolution 1.80&Aring;" />
'''TRAP4 (engineered TRAP)'''<br />
'''TRAP4 (engineered TRAP)'''<br />
==Overview==
==Overview==
-
The protein TRAP (trp RNA binding attenuation protein) forms a highly, thermostable ring-shaped 11-mer. By linking in tandem two, three, or four, DNA sequences encoding TRAP monomers, we have engineered new rings that, consist of 12 TRAP subunits and bind 12 ligand molecules. The hydrogen, bonding pattern and buried surface area within and between subunits are, essentially identical between the 11-mer and 12-mer crystal structures., Why do the artificial proteins choose to make single 12-mer rings? The, 12-mer rings are highly sterically strained by their peptide linkers and, far from thermostable. That proteins choose to adopt a strained, conformation of few subunits rather than an unstrained one with 11, subunits demonstrates the importance of entropic factors in controlling, protein-protein interactions in general.
+
The protein TRAP (trp RNA binding attenuation protein) forms a highly thermostable ring-shaped 11-mer. By linking in tandem two, three, or four DNA sequences encoding TRAP monomers, we have engineered new rings that consist of 12 TRAP subunits and bind 12 ligand molecules. The hydrogen bonding pattern and buried surface area within and between subunits are essentially identical between the 11-mer and 12-mer crystal structures. Why do the artificial proteins choose to make single 12-mer rings? The 12-mer rings are highly sterically strained by their peptide linkers and far from thermostable. That proteins choose to adopt a strained conformation of few subunits rather than an unstrained one with 11 subunits demonstrates the importance of entropic factors in controlling protein-protein interactions in general.
==About this Structure==
==About this Structure==
-
2EXT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with TRP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2EXT OCA].
+
2EXT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Geobacillus_stearothermophilus Geobacillus stearothermophilus] with <scene name='pdbligand=TRP:'>TRP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EXT OCA].
==Reference==
==Reference==
Line 13: Line 13:
[[Category: Geobacillus stearothermophilus]]
[[Category: Geobacillus stearothermophilus]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Heddle, J.G.]]
+
[[Category: Heddle, J G.]]
-
[[Category: Park, S.Y.]]
+
[[Category: Park, S Y.]]
-
[[Category: Tame, J.R.H.]]
+
[[Category: Tame, J R.H.]]
[[Category: Yamashita, I.]]
[[Category: Yamashita, I.]]
[[Category: Yokoyama, T.]]
[[Category: Yokoyama, T.]]
Line 24: Line 24:
[[Category: ring protein]]
[[Category: ring protein]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 10:12:36 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:15:37 2008''

Revision as of 15:15, 21 February 2008


2ext, resolution 1.80Å

Drag the structure with the mouse to rotate

TRAP4 (engineered TRAP)

Overview

The protein TRAP (trp RNA binding attenuation protein) forms a highly thermostable ring-shaped 11-mer. By linking in tandem two, three, or four DNA sequences encoding TRAP monomers, we have engineered new rings that consist of 12 TRAP subunits and bind 12 ligand molecules. The hydrogen bonding pattern and buried surface area within and between subunits are essentially identical between the 11-mer and 12-mer crystal structures. Why do the artificial proteins choose to make single 12-mer rings? The 12-mer rings are highly sterically strained by their peptide linkers and far from thermostable. That proteins choose to adopt a strained conformation of few subunits rather than an unstrained one with 11 subunits demonstrates the importance of entropic factors in controlling protein-protein interactions in general.

About this Structure

2EXT is a Single protein structure of sequence from Geobacillus stearothermophilus with as ligand. Full crystallographic information is available from OCA.

Reference

Rounding up: Engineering 12-membered rings from the cyclic 11-mer TRAP., Heddle JG, Yokoyama T, Yamashita I, Park SY, Tame JR, Structure. 2006 May;14(5):925-33. PMID:16698553

Page seeded by OCA on Thu Feb 21 17:15:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools