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[[Image:1opb.jpg|left|200px]]


{{Structure
==THE CRYSTAL STRUCTURES OF HOLO-AND APO-CELLULAR RETINOL BINDING PROTEIN II==
|PDB= 1opb |SIZE=350|CAPTION= <scene name='initialview01'>1opb</scene>, resolution 1.9&Aring;
<StructureSection load='1opb' size='340' side='right'caption='[[1opb]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=RET:RETINAL'>RET</scene>
<table><tr><td colspan='2'>[[1opb]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_rattus Rattus rattus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OPB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OPB FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1opb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1opb OCA], [https://pdbe.org/1opb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1opb RCSB], [https://www.ebi.ac.uk/pdbsum/1opb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1opb ProSAT]</span></td></tr>
|RELATEDENTRY=
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1opb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1opb OCA], [http://www.ebi.ac.uk/pdbsum/1opb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1opb RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/RET2_RAT RET2_RAT] Intracellular transport of retinol.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/op/1opb_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1opb ConSurf].
<div style="clear:both"></div>


'''THE CRYSTAL STRUCTURES OF HOLO-AND APO-CELLULAR RETINOL BINDING PROTEIN II'''
==See Also==
 
*[[Retinol-binding protein 3D structures|Retinol-binding protein 3D structures]]
 
__TOC__
==Overview==
</StructureSection>
Apo and holo-cellular retinol-binding protein II have been crystallized, and their crystal structures have been determined to 2.1 A and 1.9 A respectively. The apo and holo-crystals have different but related triclinic space groups. The X-ray phases for both structures were determined using the molecular replacement method. The crystal co-ordinates were refined to an R-factor of 0.200 for apo, and 0.173 for holo-cellular retinol-binding protein II. The holo and apo-models have nearly the same tertiary structures. Cellular retinol-binding protein II consists of a ten-stranded anti-parallel beta-barrel with the ligand binding cavity within the barrel. Two alpha-helices cover the open end of the beta-barrel making it almost solvent inaccessible. A single portal large enough to admit a water molecule was observed opening into the binding cavity. Exogenously added retinol was found within the cavity of each holo-cellular retinol-binding protein II molecule. Each retinol was surrounded by both polar and non-polar residues. The hydroxyl group of the bound retinol hydrogen bonds to the amide group of glutamine 108. The overall conformation of the bound retinol was derived from the four different molecules of holo-cellular retinol-binding protein II present in the triclinic form. The four copies of bound retinol had essentially the same conformation as found in crystalline retinaldehyde.
[[Category: Large Structures]]
 
[[Category: Rattus rattus]]
==About this Structure==
[[Category: Banaszak L]]
1OPB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OPB OCA].
[[Category: Winter N]]
 
==Reference==
Crystal structures of holo and apo-cellular retinol-binding protein II., Winter NS, Bratt JM, Banaszak LJ, J Mol Biol. 1993 Apr 20;230(4):1247-59. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8487303 8487303]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Banaszak, L.]]
[[Category: Winter, N.]]
[[Category: retinol transport]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:48:28 2008''

Latest revision as of 11:02, 14 February 2024

THE CRYSTAL STRUCTURES OF HOLO-AND APO-CELLULAR RETINOL BINDING PROTEIN IITHE CRYSTAL STRUCTURES OF HOLO-AND APO-CELLULAR RETINOL BINDING PROTEIN II

Structural highlights

1opb is a 4 chain structure with sequence from Rattus rattus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RET2_RAT Intracellular transport of retinol.

Evolutionary Conservation

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

See Also

1opb, resolution 1.90Å

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