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==REFINED STRUCTURE OF PORIN FROM RHODOPSEUDOMONAS BLASTICA AND COMPARISON WITH THE PORIN FROM RHODOBACTER CAPSULATUS==
==REFINED STRUCTURE OF PORIN FROM RHODOPSEUDOMONAS BLASTICA AND COMPARISON WITH THE PORIN FROM RHODOBACTER CAPSULATUS==
<StructureSection load='1prn' size='340' side='right' caption='[[1prn]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
<StructureSection load='1prn' size='340' side='right'caption='[[1prn]], [[Resolution|resolution]] 1.96&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1prn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhodobacter_blasticus Rhodobacter blasticus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PRN FirstGlance]. <br>
<table><tr><td colspan='2'>[[1prn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Fuscovulum_blasticum Fuscovulum blasticum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PRN FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</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]] 1.96&#8491;</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=1prn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1prn RCSB], [http://www.ebi.ac.uk/pdbsum/1prn PDBsum]</span></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</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=1prn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1prn OCA], [https://pdbe.org/1prn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1prn RCSB], [https://www.ebi.ac.uk/pdbsum/1prn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1prn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/PORI_RHOBL PORI_RHOBL]] Forms channels that allow the passive diffusion of small hydrophilic solutes up to an exclusion limit of about 0.6 kDa.  
[https://www.uniprot.org/uniprot/PORI_FUSBL PORI_FUSBL] Forms channels that allow the passive diffusion of small hydrophilic solutes up to an exclusion limit of about 0.6 kDa.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/1prn_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pr/1prn_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1prn ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of the membrane channel porin from the phototrophic bacteria Rhodopseudomonas blastica has been refined at 1.96 A resolution yielding an R-factor of 17.6%. The final model consists of all 289 amino acid residues, 247 water molecules and three detergent molecules modelled as n-octyltetraoxyethylene. One of these detergent molecules binds together with its two symmetry-related molecules tightly in a pocket at the molecular 3-fold axis. This pocket may bind three alkyl chains of a lipopolysaccharide which in turn would stabilize the trimer and could possibly play a role in membrane insertion. The overall shape of this porin resembles OmpF of Escherichia coli more than the only known sequence-related porin from Rhodobacter capsulatus. The membrane contacting surface is similar in all structurally known porins; it shows exceptional frequencies of amino acid residues and side-chain rotamers. The 46-residue loop beta 5-beta 6 of the porin is shown to be tightly fastened to the beta-barrel, excluding an in vivo loop movement that closes the pore. The trimer interface region has the structure of a water-soluble protein with an extensive non-polar core and numerous hydrogen bonds at the surface. The loops at the external end of the barrel are long and rigid whereas those at the periplasmic barrel end are short and mobile. The crystal packing is discussed.
Refined structure of the porin from Rhodopseudomonas blastica. Comparison with the porin from Rhodobacter capsulatus.,Kreusch A, Schulz GE J Mol Biol. 1994 Nov 11;243(5):891-905. PMID:7525973<ref>PMID:7525973</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>


==See Also==
==See Also==
*[[Porin|Porin]]
*[[Porin 3D structures|Porin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Rhodobacter blasticus]]
[[Category: Fuscovulum blasticum]]
[[Category: Kreusch, A]]
[[Category: Large Structures]]
[[Category: Schulz, G E]]
[[Category: Kreusch A]]
[[Category: Integral membrane protein porin]]
[[Category: Schulz GE]]

Latest revision as of 11:10, 14 February 2024

REFINED STRUCTURE OF PORIN FROM RHODOPSEUDOMONAS BLASTICA AND COMPARISON WITH THE PORIN FROM RHODOBACTER CAPSULATUSREFINED STRUCTURE OF PORIN FROM RHODOPSEUDOMONAS BLASTICA AND COMPARISON WITH THE PORIN FROM RHODOBACTER CAPSULATUS

Structural highlights

1prn is a 1 chain structure with sequence from Fuscovulum blasticum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.96Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PORI_FUSBL Forms channels that allow the passive diffusion of small hydrophilic solutes up to an exclusion limit of about 0.6 kDa.

Evolutionary Conservation

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

See Also

1prn, resolution 1.96Å

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