1mps: Difference between revisions
New page: left|200px<br /><applet load="1mps" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mps, resolution 2.55Å" /> '''PHOTOSYNTHETIC REACT... |
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[[Image:1mps.gif|left|200px]]<br /><applet load="1mps" size=" | [[Image:1mps.gif|left|200px]]<br /><applet load="1mps" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1mps, resolution 2.55Å" /> | caption="1mps, resolution 2.55Å" /> | ||
'''PHOTOSYNTHETIC REACTION CENTER MUTANT WITH PHE M 197 REPLACED WITH ARG AND TYR M 177 REPLACED WITH PHE (CHAIN M, Y177F, F197R)'''<br /> | '''PHOTOSYNTHETIC REACTION CENTER MUTANT WITH PHE M 197 REPLACED WITH ARG AND TYR M 177 REPLACED WITH PHE (CHAIN M, Y177F, F197R)'''<br /> | ||
==Overview== | ==Overview== | ||
Reaction centers have been crystallized from the antenna-deficient RCO2 | Reaction centers have been crystallized from the antenna-deficient RCO2 strain of Rhodobacter sphaeroides, and a structural model has been constructed at 2.6 A resolution. The antenna-deficient strain allows assessment of the structural integrity of the reaction center at each stage in the purification-crystallization procedure. Spectroscopic evidence indicates that the properties of the reaction center bacteriopheophytins and the primary donor bacteriochlorophylls are modified somewhat on removal of the protein complex from the membrane and that these changes are carried through to the crystal form of the reaction center. The structure of a FM197R/YM177F mutant reaction center has also been determined to 2.55 A resolution. The mutant complex shows an unexpected change in structure, with a significant reorientation of the new arginine, the incorporation of a new water molecule into the structure, and rotation of the 2-acetyl carbonyl group of one of the primary donor bacteriochlorophylls to a more out-of-plane geometry. Changes in the optical spectrum of the FM197R/YM177F reaction center are discussed with respect to the altered structure of the complex. | ||
==About this Structure== | ==About this Structure== | ||
1MPS 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 FE2, PO4, BCL, BPH, U10, SPN and LDA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1MPS 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=FE2:'>FE2</scene>, <scene name='pdbligand=PO4:'>PO4</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> and <scene name='pdbligand=LDA:'>LDA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MPS OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Rhodobacter sphaeroides]] | [[Category: Rhodobacter sphaeroides]] | ||
[[Category: Cogdell, R | [[Category: Cogdell, R J.]] | ||
[[Category: Fyfe, P | [[Category: Fyfe, P K.]] | ||
[[Category: Hunter, C | [[Category: Hunter, C N.]] | ||
[[Category: Isaacs, N | [[Category: Isaacs, N W.]] | ||
[[Category: Jones, M | [[Category: Jones, M R.]] | ||
[[Category: Mcauley-Hecht, K | [[Category: Mcauley-Hecht, K E.]] | ||
[[Category: Prince, S.]] | [[Category: Prince, S.]] | ||
[[Category: Ridge, J | [[Category: Ridge, J P.]] | ||
[[Category: BCL]] | [[Category: BCL]] | ||
[[Category: BPH]] | [[Category: BPH]] | ||
| Line 33: | Line 33: | ||
[[Category: transmembrane]] | [[Category: transmembrane]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:45 2008'' | ||
Revision as of 14:57, 21 February 2008
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PHOTOSYNTHETIC REACTION CENTER MUTANT WITH PHE M 197 REPLACED WITH ARG AND TYR M 177 REPLACED WITH PHE (CHAIN M, Y177F, F197R)
OverviewOverview
Reaction centers have been crystallized from the antenna-deficient RCO2 strain of Rhodobacter sphaeroides, and a structural model has been constructed at 2.6 A resolution. The antenna-deficient strain allows assessment of the structural integrity of the reaction center at each stage in the purification-crystallization procedure. Spectroscopic evidence indicates that the properties of the reaction center bacteriopheophytins and the primary donor bacteriochlorophylls are modified somewhat on removal of the protein complex from the membrane and that these changes are carried through to the crystal form of the reaction center. The structure of a FM197R/YM177F mutant reaction center has also been determined to 2.55 A resolution. The mutant complex shows an unexpected change in structure, with a significant reorientation of the new arginine, the incorporation of a new water molecule into the structure, and rotation of the 2-acetyl carbonyl group of one of the primary donor bacteriochlorophylls to a more out-of-plane geometry. Changes in the optical spectrum of the FM197R/YM177F reaction center are discussed with respect to the altered structure of the complex.
About this StructureAbout this Structure
1MPS is a Protein complex structure of sequences from Rhodobacter sphaeroides with , , , , , and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structural studies of wild-type and mutant reaction centers from an antenna-deficient strain of Rhodobacter sphaeroides: monitoring the optical properties of the complex from bacterial cell to crystal., McAuley-Hecht KE, Fyfe PK, Ridge JP, Prince SM, Hunter CN, Isaacs NW, Cogdell RJ, Jones MR, Biochemistry. 1998 Apr 7;37(14):4740-50. PMID:9537989
Page seeded by OCA on Thu Feb 21 13:57:45 2008