3blg
From Proteopedia
(Difference between revisions)
Line 3: | Line 3: | ||
<StructureSection load='3blg' size='340' side='right'caption='[[3blg]], [[Resolution|resolution]] 2.56Å' scene=''> | <StructureSection load='3blg' size='340' side='right'caption='[[3blg]], [[Resolution|resolution]] 2.56Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3blg]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3blg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BLG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BLG FirstGlance]. <br> |
- | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.56Å</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=3blg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3blg OCA], [https://pdbe.org/3blg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3blg RCSB], [https://www.ebi.ac.uk/pdbsum/3blg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3blg ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
- | [ | + | [https://www.uniprot.org/uniprot/LACB_BOVIN LACB_BOVIN] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Line 18: | Line 19: | ||
</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=3blg 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=3blg ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | The structures of the trigonal crystal form of bovine beta-lactoglobulin variant A at pH 6.2, 7.1, and 8.2 have been determined by X-ray diffraction methods at a resolution of 2.56, 2. 24, and 2.49 A, respectively. The corresponding values for R (Rfree) are 0.192 (0.240), 0.234 (0.279), and 0.232 (0.277). The C and N termini as well as two disulfide bonds are clearly defined in these models. The glutamate side chain of residue 89 is buried at pH 6.2 and becomes exposed at pH 7.1 and 8.2. This conformational change, involving the loop 85-90, provides a structural basis for a variety of pH-dependent chemical, physical, and spectroscopic phenomena, collectively known as the Tanford transition. | ||
- | |||
- | Structural basis of the Tanford transition of bovine beta-lactoglobulin.,Qin BY, Bewley MC, Creamer LK, Baker HM, Baker EN, Jameson GB Biochemistry. 1998 Oct 6;37(40):14014-23. PMID:9760236<ref>PMID:9760236</ref> | ||
- | |||
- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 3blg" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] | *[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
- | [[Category: Baker | + | [[Category: Baker EN]] |
- | [[Category: Baker | + | [[Category: Baker HM]] |
- | [[Category: Bewley | + | [[Category: Bewley MC]] |
- | [[Category: Creamer | + | [[Category: Creamer LK]] |
- | [[Category: Jameson | + | [[Category: Jameson GB]] |
- | [[Category: Qin | + | [[Category: Qin BY]] |
- | + | ||
- | + | ||
- | + | ||
- | + | ||
- | + |
Current revision
STRUCTURAL BASIS OF THE TANFORD TRANSITION OF BOVINE BETA-LACTOGLOBULIN FROM CRYSTAL STRUCTURES AT THREE PH VALUES; PH 6.2
|
Categories: Bos taurus | Large Structures | Baker EN | Baker HM | Bewley MC | Creamer LK | Jameson GB | Qin BY