2boz

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[[Image:2boz.gif|left|200px]]<br /><applet load="2boz" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2boz.gif|left|200px]]
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caption="2boz, resolution 2.40&Aring;" />
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'''PHOTOSYNTHETIC REACTION CENTER MUTANT WITH GLY M203 REPLACED WITH LEU'''<br />
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{{Structure
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|PDB= 2boz |SIZE=350|CAPTION= <scene name='initialview01'>2boz</scene>, resolution 2.40&Aring;
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|SITE= <scene name='pdbsite=AC1:U10+Binding+Site+For+Chain+L'>AC1</scene>
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|LIGAND= <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=D10:DECANE'>D10</scene>, <scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BH1:BACTERIOPHEOPHYTIN'>BH1</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene> and <scene name='pdbligand=SPN:SPEROIDENONE'>SPN</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''PHOTOSYNTHETIC REACTION CENTER MUTANT WITH GLY M203 REPLACED WITH LEU'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BOZ 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=PO4:'>PO4</scene>, <scene name='pdbligand=LDA:'>LDA</scene>, <scene name='pdbligand=D10:'>D10</scene>, <scene name='pdbligand=BCL:'>BCL</scene>, <scene name='pdbligand=BH1:'>BH1</scene>, <scene name='pdbligand=U10:'>U10</scene> and <scene name='pdbligand=SPN:'>SPN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:U10+Binding+Site+For+Chain+L'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BOZ OCA].
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2BOZ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rhodobacter_sphaeroides Rhodobacter sphaeroides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BOZ OCA].
==Reference==
==Reference==
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Strong effects of an individual water molecule on the rate of light-driven charge separation in the Rhodobacter sphaeroides reaction center., Potter JA, Fyfe PK, Frolov D, Wakeham MC, van Grondelle R, Robert B, Jones MR, J Biol Chem. 2005 Jul 22;280(29):27155-64. Epub 2005 May 20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15908429 15908429]
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Strong effects of an individual water molecule on the rate of light-driven charge separation in the Rhodobacter sphaeroides reaction center., Potter JA, Fyfe PK, Frolov D, Wakeham MC, van Grondelle R, Robert B, Jones MR, J Biol Chem. 2005 Jul 22;280(29):27155-64. Epub 2005 May 20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15908429 15908429]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rhodobacter sphaeroides]]
[[Category: Rhodobacter sphaeroides]]
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[[Category: transmembrane photosynthesis]]
[[Category: transmembrane photosynthesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:04:46 2008''

Revision as of 14:04, 20 March 2008

Image:2boz.gif


PDB ID 2boz

Drag the structure with the mouse to rotate
, resolution 2.40Å
Sites:
Ligands: , , , , , , and
Coordinates: save as pdb, mmCIF, xml



PHOTOSYNTHETIC REACTION CENTER MUTANT WITH GLY M203 REPLACED WITH LEU


Overview

The role of a water molecule (water A) located between the primary electron donor (P) and first electron acceptor bacteriochlorophyll (B(A)) in the purple bacterial reaction center was investigated by mutation of glycine M203 to leucine (GM203L). The x-ray crystal structure of the GM203L reaction center shows that the new leucine residue packs in such a way that water A is sterically excluded from the complex, but the structure of the protein-cofactor system around the mutation site is largely undisturbed. The results of absorbance and resonance Raman spectroscopy were consistent with either the removal of a hydrogen bond interaction between water A and the keto carbonyl group of B(A) or a change in the local electrostatic environment of this carbonyl group. Similarities in the spectroscopic properties and x-ray crystal structures of reaction centers with leucine and aspartic acid mutations at the M203 position suggested that the effects of a glycine to aspartic acid substitution at the M203 position can also be explained by steric exclusion of water A. In the GM203L mutant, loss of water A was accompanied by an approximately 8-fold slowing of the rate of decay of the primary donor excited state, indicating that the presence of water A is important for optimization of the rate of primary electron transfer. Possible functions of this water molecule are discussed, including a switching role in which the redox potential of the B(A) acceptor is rapidly modulated in response to oxidation of the primary electron donor.

About this Structure

2BOZ is a Protein complex structure of sequences from Rhodobacter sphaeroides. Full crystallographic information is available from OCA.

Reference

Strong effects of an individual water molecule on the rate of light-driven charge separation in the Rhodobacter sphaeroides reaction center., Potter JA, Fyfe PK, Frolov D, Wakeham MC, van Grondelle R, Robert B, Jones MR, J Biol Chem. 2005 Jul 22;280(29):27155-64. Epub 2005 May 20. PMID:15908429

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