|
|
| Line 3: |
Line 3: |
| | <StructureSection load='5orf' size='340' side='right'caption='[[5orf]], [[Resolution|resolution]] 2.54Å' scene=''> | | <StructureSection load='5orf' size='340' side='right'caption='[[5orf]], [[Resolution|resolution]] 2.54Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5orf]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ORF OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5ORF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5orf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Ovis_aries Ovis aries]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ORF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ORF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</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]] 2.54Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4luf|4luf]], [[4luh|4luh]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=PRO:PROLINE'>PRO</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5orf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5orf OCA], [http://pdbe.org/5orf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5orf RCSB], [http://www.ebi.ac.uk/pdbsum/5orf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5orf 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=5orf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5orf OCA], [https://pdbe.org/5orf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5orf RCSB], [https://www.ebi.ac.uk/pdbsum/5orf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5orf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ALBU_SHEEP ALBU_SHEEP]] Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. | + | [https://www.uniprot.org/uniprot/ALBU_SHEEP ALBU_SHEEP] Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 28: |
Line 28: |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Ovis aries]] | | [[Category: Ovis aries]] |
| - | [[Category: Bujacz, A]] | + | [[Category: Bujacz A]] |
| - | [[Category: Bujacz, G]] | + | [[Category: Bujacz G]] |
| - | [[Category: Pietrzyk-Brzezinska, A J]] | + | [[Category: Pietrzyk-Brzezinska AJ]] |
| - | [[Category: Talaj, J A]] | + | [[Category: Talaj JA]] |
| - | [[Category: Ovine serum albumin]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| - | [[Category: Triclinic system]]
| + | |
| Structural highlights
Function
ALBU_SHEEP Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.
Publication Abstract from PubMed
Serum albumin (SA) is the most abundant protein in plasma and is the main transporter of molecules in the circulatory system of all vertebrates, with applications in medicine, the pharmaceutical industry and molecular biology. It is known that albumins from different organisms vary in sequence; thus, it is important to know the impact of the amino-acid sequence on the three-dimensional structure and ligand-binding properties. Here, crystal structures of ovine (OSA) and caprine (CSA) serum albumins, isolated from sheep and goat blood, are described, as well those of their complexes with 3,5-diiodosalicylic acid (DIS): OSA-DIS (2.20 A resolution) and CSA-DIS (1.78 A resolution). The ligand-free OSA structure was determined in the trigonal space group P3221 at 2.30 A resolution, while that of CSA in the orthorhombic space group P212121 was determined at 1.94 A resolution. Both albumins are also capable of crystallizing in the triclinic space group P1, giving isostructural crystals that diffract to around 2.5 A resolution. A comparison of OSA and CSA with the closely related bovine serum albumin (BSA) shows both similarities and differences in the distribution of DIS binding sites. The investigated serum albumins from domesticated ruminants in their complexes with DIS are also compared with the analogous structures of equine and human serum albumins (ESA-DIS and HSA-DIS). Surprisingly, despite 98% sequence similarity, OSA binds only two molecules of DIS, whereas CSA binds six molecules of this ligand. Moreover, the binding of DIS to OSA and CSA introduced changes in the overall architecture of the proteins, causing not only different conformations of the amino-acid side chains in the binding pockets, but also a significant shift of the whole helices, changing the volume of the binding cavities.
Crystal structures of serum albumins from domesticated ruminants and their complexes with 3,5-diiodosalicylic acid.,Bujacz A, Talaj JA, Zielinski K, Pietrzyk-Brzezinska AJ, Neumann P Acta Crystallogr D Struct Biol. 2017 Nov 1;73(Pt 11):896-909. doi:, 10.1107/S205979831701470X. Epub 2017 Oct 25. PMID:29095162[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bujacz A, Talaj JA, Zielinski K, Pietrzyk-Brzezinska AJ, Neumann P. Crystal structures of serum albumins from domesticated ruminants and their complexes with 3,5-diiodosalicylic acid. Acta Crystallogr D Struct Biol. 2017 Nov 1;73(Pt 11):896-909. doi:, 10.1107/S205979831701470X. Epub 2017 Oct 25. PMID:29095162 doi:http://dx.doi.org/10.1107/S205979831701470X
|
