1yf6

From Proteopedia

(Difference between revisions)

Revision as of 16:51, 20 October 2021

Structure of a quintuple mutant of photosynthetic reaction center from rhodobacter sphaeroides

Structural highlights

1yf6 is a 3 chain structure with sequence from "luteovulum_sphaeroides"_(van_niel_1944)_suresh_et_al._2019 "luteovulum sphaeroides" (van niel 1944) suresh et al. 2019. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , , , , , ,
Related:	1rzh, 1qov
Gene:	pufL ("Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019), pufM ("Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019), puhA ("Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RCEL_RHOSH] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [RCEH_RHOSH] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [RCEM_RHOSH] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The photosynthetic reaction center (RC) from purple bacteria converts light into chemical energy. Although the RC shows two nearly structurally symmetric branches, A and B, light-induced electron transfer in the native RC occurs almost exclusively along the A-branch to a primary quinone electron acceptor Q(A). Subsequent electron and proton transfer to a mobile quinone molecule Q(B) converts it to a quinol, Q(B)H(2). We report the construction and characterization of a series of mutants in Rhodobacter sphaeroides designed to reduce Q(B) via the B-branch. The quantum efficiency to Q(B) via the B-branch Phi(B) ranged from 0.4% in an RC containing the single mutation Ala-M260 --> Trp to 5% in a quintuple mutant which includes in addition three mutations to inhibit transfer along the A-branch (Gly-M203 --> Asp, Tyr-M210 --> Phe, Leu-M214 --> His) and one to promote transfer along the B-branch (Phe-L181 --> Tyr). Comparing the value of 0.4% for Phi(B) obtained in the AW(M260) mutant, which lacks Q(A), to the 100% quantum efficiency for Phi(A) along the A-branch in the native RC, we obtain a ratio for A-branch to B-branch electron transfer of 250:1. We determined the structure of the most effective (quintuple) mutant RC at 2.25 A (R-factor = 19.6%). The Q(A) site did not contain a quinone but was occupied by the side chain of Trp-M260 and a Cl(-). In this structure a nonfunctional quinone was found to occupy a new site near M258 and M268. The implications of this work to trap intermediate states are discussed.

Quinone (QB) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: quantum efficiency and X-ray structure.,Paddock ML, Chang C, Xu Q, Abresch EC, Axelrod HL, Feher G, Okamura MY Biochemistry. 2005 May 10;44(18):6920-8. PMID:15865437^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Paddock ML, Chang C, Xu Q, Abresch EC, Axelrod HL, Feher G, Okamura MY. Quinone (QB) reduction by B-branch electron transfer in mutant bacterial reaction centers from Rhodobacter sphaeroides: quantum efficiency and X-ray structure. Biochemistry. 2005 May 10;44(18):6920-8. PMID:15865437 doi:10.1021/bi047559m

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1yf6"

@@ Line 3: / Line 3: @@
 <StructureSection load='1yf6' size='340' side='right'caption='[[1yf6]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1yf6]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/"rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YF6 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1YF6 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1yf6]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/"luteovulum_sphaeroides"_(van_niel_1944)_suresh_et_al._2019 "luteovulum sphaeroides" (van niel 1944) suresh et al. 2019]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YF6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YF6 FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPH:BACTERIOPHEOPHYTIN+A'>BPH</scene>, <scene name='pdbligand=CDL:CARDIOLIPIN'>CDL</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HTO:HEPTANE-1,2,3-TRIOL'>HTO</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SPO:SPHEROIDENE'>SPO</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1rzh|1rzh]], [[1qov|1qov]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pufL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907]), pufM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907]), puhA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pufL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019]), pufM ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019]), puhA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Luteovulum sphaeroides" (van Niel 1944) Suresh et al. 2019])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1yf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yf6 OCA], [http://pdbe.org/1yf6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1yf6 RCSB], [http://www.ebi.ac.uk/pdbsum/1yf6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1yf6 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1yf6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1yf6 OCA], [https://pdbe.org/1yf6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1yf6 RCSB], [https://www.ebi.ac.uk/pdbsum/1yf6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1yf6 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/RCEL_RHOSH RCEL_RHOSH]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [[http://www.uniprot.org/uniprot/RCEH_RHOSH RCEH_RHOSH]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [[http://www.uniprot.org/uniprot/RCEM_RHOSH RCEM_RHOSH]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
+[[https://www.uniprot.org/uniprot/RCEL_RHOSH RCEL_RHOSH]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [[https://www.uniprot.org/uniprot/RCEH_RHOSH RCEH_RHOSH]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [[https://www.uniprot.org/uniprot/RCEM_RHOSH RCEM_RHOSH]] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 34: / Line 34: @@
 __TOC__
 </StructureSection>
-[[Category: Rhodococcus capsulatus molisch 1907]]
 [[Category: Large Structures]]
 [[Category: Abresch, E C]]

1yf6

From Proteopedia

Revision as of 16:51, 20 October 2021

Structure of a quintuple mutant of photosynthetic reaction center from rhodobacter sphaeroides

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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