This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1umx

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 09:41, 29 September 2021

PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ARG M267 REPLACED WITH LEU (CHAIN M, R267L)

Structural highlights

1umx 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:	1aig, 1aij, 1ds8, 1dv3, 1dv6, 1e14, 1e6d, 1f6n, 1fnp, 1fnq, 1jgw, 1jgx, 1jgy, 1jgz, 1jh0, 1k6l, 1k6n, 1kby, 1l9b, 1l9j, 1m3x, 1mps, 1ogv, 1pcr, 1pss, 1pst, 1qov, 1yst, 2rcr, 4rcr
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.

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

Relatively little is known about the functions of specific molecular interactions between membrane proteins and membrane lipids. The structural and functional consequences of disrupting a previously identified interaction between a molecule of the diacidic lipid cardiolipin and the purple bacterial reaction centre were examined. Mutagenesis of a highly conserved arginine (M267) that is responsible for binding the head-group of the cardiolipin (to leucine) did not affect the rate of photosynthetic growth, the functional properties of the reaction centre, or the X-ray crystal structure of the complex (determined to a resolution of 2.8 A). However, the thermal stability of the protein was compromised by this mutation, part of the reaction centre population showing an approximately 5 degrees C decrease in melting temperature in response to the arginine to leucine mutation. The crystallised mutant reaction centre also no longer bound detectable amounts of cardiolipin at this site. Taken together, these observations suggest that this particular protein-lipid interaction contributes to the thermal stability of the complex, at least when in detergent micelles. These findings are discussed in the light of proposals concerning the unfolding processes that occur when membrane proteins are heated, and we propose that one function of the cardiolipin is to stabilise the interaction between adjacent membrane-spanning alpha-helices in a region where there are no direct protein-protein interactions.

Disruption of a specific molecular interaction with a bound lipid affects the thermal stability of the purple bacterial reaction centre.,Fyfe PK, Isaacs NW, Cogdell RJ, Jones MR Biochim Biophys Acta. 2004 Jan 30;1608(1):11-22. PMID:14741581^[1]

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

References

↑ Fyfe PK, Isaacs NW, Cogdell RJ, Jones MR. Disruption of a specific molecular interaction with a bound lipid affects the thermal stability of the purple bacterial reaction centre. Biochim Biophys Acta. 2004 Jan 30;1608(1):11-22. PMID:14741581

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/1umx"

@@ Line 3: / Line 3: @@
 <StructureSection load='1umx' size='340' side='right'caption='[[1umx]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1umx]] 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=1UMX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UMX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1umx]] is a 3 chain structure with sequence from [https://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=1UMX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UMX FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BCL:BACTERIOCHLOROPHYLL+A'>BCL</scene>, <scene name='pdbligand=BPB:BACTERIOPHEOPHYTIN+B'>BPB</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SPN:SPEROIDENONE'>SPN</scene>, <scene name='pdbligand=U10:UBIQUINONE-10'>U10</scene></td></tr>
+</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=BPB:BACTERIOPHEOPHYTIN+B'>BPB</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=SPN:SPEROIDENONE'>SPN</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">[[1aig|1aig]], [[1aij|1aij]], [[1ds8|1ds8]], [[1dv3|1dv3]], [[1dv6|1dv6]], [[1e14|1e14]], [[1e6d|1e6d]], [[1f6n|1f6n]], [[1fnp|1fnp]], [[1fnq|1fnq]], [[1jgw|1jgw]], [[1jgx|1jgx]], [[1jgy|1jgy]], [[1jgz|1jgz]], [[1jh0|1jh0]], [[1k6l|1k6l]], [[1k6n|1k6n]], [[1kby|1kby]], [[1l9b|1l9b]], [[1l9j|1l9j]], [[1m3x|1m3x]], [[1mps|1mps]], [[1ogv|1ogv]], [[1pcr|1pcr]], [[1pss|1pss]], [[1pst|1pst]], [[1qov|1qov]], [[1yst|1yst]], [[2rcr|2rcr]], [[4rcr|4rcr]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1aig|1aig]], [[1aij|1aij]], [[1ds8|1ds8]], [[1dv3|1dv3]], [[1dv6|1dv6]], [[1e14|1e14]], [[1e6d|1e6d]], [[1f6n|1f6n]], [[1fnp|1fnp]], [[1fnq|1fnq]], [[1jgw|1jgw]], [[1jgx|1jgx]], [[1jgy|1jgy]], [[1jgz|1jgz]], [[1jh0|1jh0]], [[1k6l|1k6l]], [[1k6n|1k6n]], [[1kby|1kby]], [[1l9b|1l9b]], [[1l9j|1l9j]], [[1m3x|1m3x]], [[1mps|1mps]], [[1ogv|1ogv]], [[1pcr|1pcr]], [[1pss|1pss]], [[1pst|1pst]], [[1qov|1qov]], [[1yst|1yst]], [[2rcr|2rcr]], [[4rcr|4rcr]]</div></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=1umx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umx OCA], [http://pdbe.org/1umx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1umx RCSB], [http://www.ebi.ac.uk/pdbsum/1umx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1umx 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=1umx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1umx OCA], [https://pdbe.org/1umx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1umx RCSB], [https://www.ebi.ac.uk/pdbsum/1umx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1umx ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[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. [[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.
+[[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. [[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.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1umx

From Proteopedia

Revision as of 09:41, 29 September 2021

PHOTOSYNTHETIC REACTION CENTER MUTANT WITH ARG M267 REPLACED WITH LEU (CHAIN M, R267L)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox