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4n7l

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Revision as of 11:43, 5 August 2016

Zinc Substituted Reaction Center M(L214H) Variant of Rhodobacter sphaeroides

Structural highlights

4n7l is a 3 chain structure with sequence from "rhodococcus_capsulatus"_molisch_1907 "rhodococcus capsulatus" molisch 1907. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , , , , , , , , ,
Related:	4n7k
Gene:	puhA, puhApufML ("Rhodococcus capsulatus" Molisch 1907), pufL, puhApufML ("Rhodococcus capsulatus" Molisch 1907), pufM, puhApufML ("Rhodococcus capsulatus" Molisch 1907)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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

Publication Abstract from PubMed

The Zn-BChl-containing reaction center (RC) produced in a bchD (magnesium chelatase) mutant of Rhodobacter sphaeroides assembles with six Zn-bacteriochlorophylls (Zn-BChls) in place of four Mg-containing bacteriochlorophylls (BChls) and two bacteriopheophytins (BPhes). This protein presents unique opportunities for studying biological electron transfer, as Zn-containing chlorins can exist in 4-, 5-, and (theoretically) 6-coordinate states within the RC. In this paper, the electron transfer perturbations attributed exclusively to coordination state effects are separated from those attributed to the presence, absence, or type of metal in the bacteriochlorin at the HA pocket of the RC. The presence of a 4-coordinate Zn2+ ion in the HA bacteriochlorin instead of BPhe results in a small decrease in the rates of the P*-->P+HA--->P+QA- electron transfer, and the charge separation yield is not greatly perturbed; however coordination of the Zn2+ by a fifth ligand provided by a histidine residue results in a larger rate decrease and yield loss. We also report the first crystal structure of a Zn-BChl-containing RC, confirming that the HA Zn-BChl was either 4- or 5-coordinate in the two types of Zn-BChl-containing RCs studied here. Interestingly, a large degree of disorder, in combination with a relatively weak anomalous difference electron density was found in the HB pocket. These data, in combination with spectroscopic results, indicate partial occupancy of this binding pocket. These findings provide insights into the use of BPhe as the bacteriochlorin pigment of choice at HA in both BChl- and Zn-BChl-containing RCs found in nature.

Structural and kinetic properties of Rhodobacter sphaeroides photosynthetic reaction centers containing exclusively Zn-coordinated bacteriochlorophyll as bacteriochlorin cofactors.,Saer RG, Pan J, Hardjasa A, Lin S, Rosell F, Mauk AG, Woodbury NW, Murphy ME, Beatty JT Biochim Biophys Acta. 2013 Dec 5;1837(3):366-374. doi:, 10.1016/j.bbabio.2013.11.015. PMID:24316146^[1]

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

References

↑ Saer RG, Pan J, Hardjasa A, Lin S, Rosell F, Mauk AG, Woodbury NW, Murphy ME, Beatty JT. Structural and kinetic properties of Rhodobacter sphaeroides photosynthetic reaction centers containing exclusively Zn-coordinated bacteriochlorophyll as bacteriochlorin cofactors. Biochim Biophys Acta. 2013 Dec 5;1837(3):366-374. doi:, 10.1016/j.bbabio.2013.11.015. PMID:24316146 doi:http://dx.doi.org/10.1016/j.bbabio.2013.11.015

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4n7l"

Categories: Rhodococcus capsulatus molisch 1907 | Hardjasa, A | Murphy, M E.P | Photosynthesis

@@ Line 1: / Line 1: @@
 ==Zinc Substituted Reaction Center M(L214H) Variant of Rhodobacter sphaeroides==
 <StructureSection load='4n7l' size='340' side='right' caption='[[4n7l]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4n7k|4n7k]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">puhA, puhApufML ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907]), pufL, puhApufML ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907]), pufM, puhApufML ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1063 "Rhodococcus capsulatus" Molisch 1907])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4n7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n7l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n7l RCSB], [http://www.ebi.ac.uk/pdbsum/4n7l PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4n7l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n7l OCA], [http://pdbe.org/4n7l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n7l RCSB], [http://www.ebi.ac.uk/pdbsum/4n7l PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n7l ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4n7l" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

4n7l

From Proteopedia

Revision as of 11:43, 5 August 2016

Zinc Substituted Reaction Center M(L214H) Variant of Rhodobacter sphaeroides

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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