1g7k

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1g7k" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g7k, resolution 2.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
Line 1: Line 1:
-
[[Image:1g7k.gif|left|200px]]<br /><applet load="1g7k" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1g7k.gif|left|200px]]<br /><applet load="1g7k" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1g7k, resolution 2.0&Aring;" />
caption="1g7k, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE OF DSRED, A RED FLUORESCENT PROTEIN FROM DISCOSOMA SP. RED'''<br />
'''CRYSTAL STRUCTURE OF DSRED, A RED FLUORESCENT PROTEIN FROM DISCOSOMA SP. RED'''<br />
==Overview==
==Overview==
-
The crystal structure of DsRed, a red fluorescent protein from a, corallimorpharian, has been determined at 2.0-A resolution by, multiple-wavelength anomalous dispersion and crystallographic refinement., Crystals of the selenomethionine-substituted protein have space group, P2(1) and contain a tetramer with 222 noncrystallographic symmetry in the, asymmetric unit. The refined model has satisfactory stereochemistry and a, final crystallographic R factor of 0.162. The protein, which forms an, obligatory tetramer in solution and in the crystal, is a squat rectangular, prism comprising four protomers whose fold is extremely similar to that of, the Aequorea victoria green fluorescent protein despite low (, approximately 23%) amino acid sequence homology. The monomer consists of, an 11-stranded beta barrel with a coaxial helix. The chromophores, formed, from the primary sequence -Gln-Tyr-Gly- (residues 66-68), are arranged in, a approximately 27 x 34-A rectangular array in two approximately, antiparallel pairs. The geometry at the alpha carbon of Gln-66 (refined, without stereochemical restraints) is consistent with an sp(2) hybridized, center, in accord with the proposal that red fluorescence is because of an, additional oxidation step that forms an acylimine extension to the, chromophore [Gross, L. A., Baird, G. S., Hoffman, R. C., Baldridge, K. K., &amp; Tsien, R. Y. (2000) Proc. Natl. Acad. Sci. USA 87, 11990-11995]. The, carbonyl oxygen of Phe-65 is almost 90 degrees out of the plane of the, chromophore, consistent with theoretical calculations suggesting that this, is the minimum energy conformation of this moiety despite the conjugation, of this group with the rest of the chromophore.
+
The crystal structure of DsRed, a red fluorescent protein from a corallimorpharian, has been determined at 2.0-A resolution by multiple-wavelength anomalous dispersion and crystallographic refinement. Crystals of the selenomethionine-substituted protein have space group P2(1) and contain a tetramer with 222 noncrystallographic symmetry in the asymmetric unit. The refined model has satisfactory stereochemistry and a final crystallographic R factor of 0.162. The protein, which forms an obligatory tetramer in solution and in the crystal, is a squat rectangular prism comprising four protomers whose fold is extremely similar to that of the Aequorea victoria green fluorescent protein despite low ( approximately 23%) amino acid sequence homology. The monomer consists of an 11-stranded beta barrel with a coaxial helix. The chromophores, formed from the primary sequence -Gln-Tyr-Gly- (residues 66-68), are arranged in a approximately 27 x 34-A rectangular array in two approximately antiparallel pairs. The geometry at the alpha carbon of Gln-66 (refined without stereochemical restraints) is consistent with an sp(2) hybridized center, in accord with the proposal that red fluorescence is because of an additional oxidation step that forms an acylimine extension to the chromophore [Gross, L. A., Baird, G. S., Hoffman, R. C., Baldridge, K. K. &amp; Tsien, R. Y. (2000) Proc. Natl. Acad. Sci. USA 87, 11990-11995]. The carbonyl oxygen of Phe-65 is almost 90 degrees out of the plane of the chromophore, consistent with theoretical calculations suggesting that this is the minimum energy conformation of this moiety despite the conjugation of this group with the rest of the chromophore.
==About this Structure==
==About this Structure==
-
1G7K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Discosoma_sp. Discosoma sp.]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G7K OCA].
+
1G7K is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Discosoma_sp. Discosoma sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G7K OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Kallio, K.]]
[[Category: Kallio, K.]]
-
[[Category: Matz, M.V.]]
+
[[Category: Matz, M V.]]
-
[[Category: Remington, S.J.]]
+
[[Category: Remington, S J.]]
-
[[Category: Wachter, R.M.]]
+
[[Category: Wachter, R M.]]
[[Category: Yarbrough, D.]]
[[Category: Yarbrough, D.]]
[[Category: beta barrel]]
[[Category: beta barrel]]
Line 27: Line 27:
[[Category: red]]
[[Category: red]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:47:02 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:58 2008''

Revision as of 10:47, 21 February 2008

Image:1g7k.gif

1g7k, resolution 2.0Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF DSRED, A RED FLUORESCENT PROTEIN FROM DISCOSOMA SP. RED

Overview

The crystal structure of DsRed, a red fluorescent protein from a corallimorpharian, has been determined at 2.0-A resolution by multiple-wavelength anomalous dispersion and crystallographic refinement. Crystals of the selenomethionine-substituted protein have space group P2(1) and contain a tetramer with 222 noncrystallographic symmetry in the asymmetric unit. The refined model has satisfactory stereochemistry and a final crystallographic R factor of 0.162. The protein, which forms an obligatory tetramer in solution and in the crystal, is a squat rectangular prism comprising four protomers whose fold is extremely similar to that of the Aequorea victoria green fluorescent protein despite low ( approximately 23%) amino acid sequence homology. The monomer consists of an 11-stranded beta barrel with a coaxial helix. The chromophores, formed from the primary sequence -Gln-Tyr-Gly- (residues 66-68), are arranged in a approximately 27 x 34-A rectangular array in two approximately antiparallel pairs. The geometry at the alpha carbon of Gln-66 (refined without stereochemical restraints) is consistent with an sp(2) hybridized center, in accord with the proposal that red fluorescence is because of an additional oxidation step that forms an acylimine extension to the chromophore [Gross, L. A., Baird, G. S., Hoffman, R. C., Baldridge, K. K. & Tsien, R. Y. (2000) Proc. Natl. Acad. Sci. USA 87, 11990-11995]. The carbonyl oxygen of Phe-65 is almost 90 degrees out of the plane of the chromophore, consistent with theoretical calculations suggesting that this is the minimum energy conformation of this moiety despite the conjugation of this group with the rest of the chromophore.

About this Structure

1G7K is a Single protein structure of sequence from Discosoma sp.. Full crystallographic information is available from OCA.

Reference

Refined crystal structure of DsRed, a red fluorescent protein from coral, at 2.0-A resolution., Yarbrough D, Wachter RM, Kallio K, Matz MV, Remington SJ, Proc Natl Acad Sci U S A. 2001 Jan 16;98(2):462-7. PMID:11209050

Page seeded by OCA on Thu Feb 21 12:46:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g7k"
Personal tools