1e14: Difference between revisions

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[[Image:1e14.gif|left|200px]]<br /><applet load="1e14" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1e14.gif|left|200px]]<br /><applet load="1e14" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1e14, resolution 2.7Å" />

'''PHOTOSYNTHETIC REACTION CENTER MUTANT WITH PHE M197 REPLACED WITH ARG (CHAIN M, FM197R) AND GLY M203 REPLACED WITH ASP (CHAIN M, GM203D)'''<br />

==Overview==

Reaction centers with the double mutation Phe M197 to Arg and Gly M203 to, Asp (FM197R/GM203D) have been crystallized from an antenna-deficient, strain of Rhodobacter sphaeroides, and the structure has been determined, at 2.7 A resolution. Unlike in reaction centers with a single FM197R, mutation, the Arg M197 residue in the FM197R/GM203D reaction center adopts, a position similar to that of the native Phe residue in the wild-type, reaction center. Asp M203 is packed in such a way that the gamma-carboxy, group interacts with the backbone carbonyl of Arg M197. The Asp M203, residue takes up part of the volume that is occupied in the wild-type, reaction center by a water molecule. This water has been proposed to form, a hydrogen bond interaction with the 9-keto carbonyl group of the active, branch accessory bacteriochlorophyll, particularly when the primary donor, bacteriochlorophylls are oxidized. The GM203D mutation therefore appears, to remove the possibility of this hydrogen bond interaction by exclusion, of this water molecule, as well as altering the local dielectric, environment of the 9-keto carbonyl group. We examine whether the observed, structural changes can provide new or alternative explanations for the, absorbance and electron-transfer properties of reaction centers with the, FM197R and GM203D mutations.

Reaction centers with the double mutation Phe M197 to Arg and Gly M203 to Asp (FM197R/GM203D) have been crystallized from an antenna-deficient strain of Rhodobacter sphaeroides, and the structure has been determined at 2.7 A resolution. Unlike in reaction centers with a single FM197R mutation, the Arg M197 residue in the FM197R/GM203D reaction center adopts a position similar to that of the native Phe residue in the wild-type reaction center. Asp M203 is packed in such a way that the gamma-carboxy group interacts with the backbone carbonyl of Arg M197. The Asp M203 residue takes up part of the volume that is occupied in the wild-type reaction center by a water molecule. This water has been proposed to form a hydrogen bond interaction with the 9-keto carbonyl group of the active branch accessory bacteriochlorophyll, particularly when the primary donor bacteriochlorophylls are oxidized. The GM203D mutation therefore appears to remove the possibility of this hydrogen bond interaction by exclusion of this water molecule, as well as altering the local dielectric environment of the 9-keto carbonyl group. We examine whether the observed structural changes can provide new or alternative explanations for the absorbance and electron-transfer properties of reaction centers with the FM197R and GM203D mutations.

==About this Structure==

1E14 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with FE, BCL, BPH, U10, SPN, LDA and CDL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1E14 OCA].

1E14 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=BCL:'>BCL</scene>, <scene name='pdbligand=BPH:'>BPH</scene>, <scene name='pdbligand=U10:'>U10</scene>, <scene name='pdbligand=SPN:'>SPN</scene>, <scene name='pdbligand=LDA:'>LDA</scene> and <scene name='pdbligand=CDL:'>CDL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E14 OCA].

==Reference==

Line 13:

[[Category: Protein complex]]

[[Category: Rhodobacter sphaeroides]]

[[Category: Cogdell, R.J.]]

[[Category: Cogdell, R J.]]

[[Category: Fyfe, P.K.]]

[[Category: Fyfe, P K.]]

[[Category: Isaacs, N.W.]]

[[Category: Isaacs, N W.]]

[[Category: Jones, M.R.]]

[[Category: Jones, M R.]]

[[Category: Mcauley, K.E.]]

[[Category: Mcauley, K E.]]

[[Category: Ridge, J.P.]]

[[Category: Ridge, J P.]]

[[Category: BCL]]

[[Category: BPH]]

Line 31:

[[Category: transmembrane]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Tue Nov 20 13~~:43:~~28 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:38 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1e14.gif|left|200px]]<br /><applet load="1e14" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1e14.gif|left|200px]]<br /><applet load="1e14" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1e14, resolution 2.7&Aring;" />
 '''PHOTOSYNTHETIC REACTION CENTER MUTANT WITH PHE M197 REPLACED WITH ARG (CHAIN M, FM197R) AND GLY M203 REPLACED WITH ASP (CHAIN M, GM203D)'''<br />
 ==Overview==
-Reaction centers with the double mutation Phe M197 to Arg and Gly M203 to, Asp (FM197R/GM203D) have been crystallized from an antenna-deficient, strain of Rhodobacter sphaeroides, and the structure has been determined, at 2.7 A resolution. Unlike in reaction centers with a single FM197R, mutation, the Arg M197 residue in the FM197R/GM203D reaction center adopts, a position similar to that of the native Phe residue in the wild-type, reaction center. Asp M203 is packed in such a way that the gamma-carboxy, group interacts with the backbone carbonyl of Arg M197. The Asp M203, residue takes up part of the volume that is occupied in the wild-type, reaction center by a water molecule. This water has been proposed to form, a hydrogen bond interaction with the 9-keto carbonyl group of the active, branch accessory bacteriochlorophyll, particularly when the primary donor, bacteriochlorophylls are oxidized. The GM203D mutation therefore appears, to remove the possibility of this hydrogen bond interaction by exclusion, of this water molecule, as well as altering the local dielectric, environment of the 9-keto carbonyl group. We examine whether the observed, structural changes can provide new or alternative explanations for the, absorbance and electron-transfer properties of reaction centers with the, FM197R and GM203D mutations.
+Reaction centers with the double mutation Phe M197 to Arg and Gly M203 to Asp (FM197R/GM203D) have been crystallized from an antenna-deficient strain of Rhodobacter sphaeroides, and the structure has been determined at 2.7 A resolution. Unlike in reaction centers with a single FM197R mutation, the Arg M197 residue in the FM197R/GM203D reaction center adopts a position similar to that of the native Phe residue in the wild-type reaction center. Asp M203 is packed in such a way that the gamma-carboxy group interacts with the backbone carbonyl of Arg M197. The Asp M203 residue takes up part of the volume that is occupied in the wild-type reaction center by a water molecule. This water has been proposed to form a hydrogen bond interaction with the 9-keto carbonyl group of the active branch accessory bacteriochlorophyll, particularly when the primary donor bacteriochlorophylls are oxidized. The GM203D mutation therefore appears to remove the possibility of this hydrogen bond interaction by exclusion of this water molecule, as well as altering the local dielectric environment of the 9-keto carbonyl group. We examine whether the observed structural changes can provide new or alternative explanations for the absorbance and electron-transfer properties of reaction centers with the FM197R and GM203D mutations.
 ==About this Structure==
-E14 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with FE, BCL, BPH, U10, SPN, LDA and CDL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1E14 OCA].
+E14 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides] with <scene name='pdbligand=FE:'>FE</scene>, <scene name='pdbligand=BCL:'>BCL</scene>, <scene name='pdbligand=BPH:'>BPH</scene>, <scene name='pdbligand=U10:'>U10</scene>, <scene name='pdbligand=SPN:'>SPN</scene>, <scene name='pdbligand=LDA:'>LDA</scene> and <scene name='pdbligand=CDL:'>CDL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E14 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Protein complex]]
 [[Category: Rhodobacter sphaeroides]]
-[[Category: Cogdell, R.J.]]
+[[Category: Cogdell, R J.]]
-[[Category: Fyfe, P.K.]]
+[[Category: Fyfe, P K.]]
-[[Category: Isaacs, N.W.]]
+[[Category: Isaacs, N W.]]
-[[Category: Jones, M.R.]]
+[[Category: Jones, M R.]]
-[[Category: Mcauley, K.E.]]
+[[Category: Mcauley, K E.]]
-[[Category: Ridge, J.P.]]
+[[Category: Ridge, J P.]]
 [[Category: BCL]]
 [[Category: BPH]]
@@ Line 31: / Line 31: @@
 [[Category: transmembrane]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 13:43:28 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:22:38 2008''