1mgy

From Proteopedia

(Difference between revisions)

Current revision

Structure of the D85S mutant of bacteriorhodopsin with bromide bound

Structural highlights

1mgy is a 1 chain structure with sequence from Halobacterium salinarum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2Å
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BACR_HALSA Light-driven proton pump.

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

We report the crystal structure of a bromide-bound form of the D85S mutant of bacteriorhodopsin, bR(D85S), a protein that uses light energy rather than ATP to pump halide ions across the cell membrane. Comparison of the structure of the halide-bound and halide-free states reveals that both displacements of individual side-chain positions and concerted helical movements occur on the extracellular side of the protein. Analysis of these structural changes reveals how this ion pump first facilitates ion uptake deep within the cell membrane and then prevents the backward escape of ions later in the pumping cycle. Together with the information provided by structures of intermediate states in the bacteriorhodopsin photocycle, this study also suggests the overall design principles that are necessary for ion pumping.

Crystal structure of the bromide-bound D85S mutant of bacteriorhodopsin: principles of ion pumping.,Facciotti MT, Cheung VS, Nguyen D, Rouhani S, Glaeser RM Biophys J. 2003 Jul;85(1):451-8. PMID:12829500^[1]

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

References

↑ Facciotti MT, Cheung VS, Nguyen D, Rouhani S, Glaeser RM. Crystal structure of the bromide-bound D85S mutant of bacteriorhodopsin: principles of ion pumping. Biophys J. 2003 Jul;85(1):451-8. PMID:12829500

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <StructureSection load='1mgy' size='340' side='right'caption='[[1mgy]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mgy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_halobius_ruber"_klebahn_1919 "bacillus halobius ruber" klebahn 1919]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MGY FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mgy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MGY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MGY FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LI1:1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL'>LI1</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=LI1:1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL'>LI1</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></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=1mgy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mgy OCA], [https://pdbe.org/1mgy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mgy RCSB], [https://www.ebi.ac.uk/pdbsum/1mgy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mgy ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA]] Light-driven proton pump.
+[https://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA] Light-driven proton pump.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 14: / Line 15: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mg/1mgy_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 35: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Bacillus halobius ruber klebahn 1919]]
+[[Category: Halobacterium salinarum]]
 [[Category: Large Structures]]
-[[Category: Cheung, V S]]
+[[Category: Cheung VS]]
-[[Category: Facciotti, M T]]
+[[Category: Facciotti MT]]
-[[Category: Glaeser, R M]]
+[[Category: Glaeser RM]]
-[[Category: Nguyen, D]]
+[[Category: Nguyen D]]
-[[Category: Rouhani, S]]
+[[Category: Rouhani S]]
-[[Category: Anion]]
-[[Category: Bacteriorhodopsin]]
-[[Category: Bromide]]
-[[Category: Halide]]
-[[Category: Proton transport]]
-[[Category: Pump]]

1mgy

From Proteopedia

Current revision

Structure of the D85S mutant of bacteriorhodopsin with bromide bound

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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