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== | ==STRUCTURE OF AN ALBUMIN-BINDING DOMAIN, NMR, 20 STRUCTURES== | ||
<StructureSection load='1gab' size='340' side='right'caption='[[1gab]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1gab]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Finegoldia_magna_ATCC_29328 Finegoldia magna ATCC 29328]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GAB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GAB FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1gab FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gab OCA], [https://pdbe.org/1gab PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gab RCSB], [https://www.ebi.ac.uk/pdbsum/1gab PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gab ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PAB_FINMA PAB_FINMA] Binds serum albumin. | |||
== 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/ga/1gab_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=1gab ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The albumin-binding GA module is found in a family of surface proteins of different bacterial species. It comprises 45 amino acid residues and represents the first known example of contemporary module shuffling. Using 1H NMR spectroscopy we have determined the solution structure of the GA module from protein PAB, a protein of the anaerobic human commensal and pathogen Peptostreptococcus magnus. This structure, the first three-dimensional structure of an albumin-binding protein domain described, was shown to be composed of a left-handed three-helix-bundle. Sequence differences between GA modules with different affinities for albumin indicated that a conserved region in the C-terminal part of the second helix and the flexible sequence between helices 2 and 3 could contribute to the albumin-binding activity. The effect on backbone amide proton exchange rates upon binding to albumin support this assumption. The GA module has a fold that is strikingly similar to the immunoglobulin-binding domains of staphylococcal protein A but it shows no resemblance to the fold shared by the immunoglobulin-binding domains of streptococcal protein G and peptostreptococcal protein L. When the gene sequences, binding properties and thermal stability of these four domains are analysed in relation to their global folds an evolutionary pattern emerges. Thus, in the evolution of novel binding properties mutations are allowed only as long as the energetically favourable global fold is maintained. | The albumin-binding GA module is found in a family of surface proteins of different bacterial species. It comprises 45 amino acid residues and represents the first known example of contemporary module shuffling. Using 1H NMR spectroscopy we have determined the solution structure of the GA module from protein PAB, a protein of the anaerobic human commensal and pathogen Peptostreptococcus magnus. This structure, the first three-dimensional structure of an albumin-binding protein domain described, was shown to be composed of a left-handed three-helix-bundle. Sequence differences between GA modules with different affinities for albumin indicated that a conserved region in the C-terminal part of the second helix and the flexible sequence between helices 2 and 3 could contribute to the albumin-binding activity. The effect on backbone amide proton exchange rates upon binding to albumin support this assumption. The GA module has a fold that is strikingly similar to the immunoglobulin-binding domains of staphylococcal protein A but it shows no resemblance to the fold shared by the immunoglobulin-binding domains of streptococcal protein G and peptostreptococcal protein L. When the gene sequences, binding properties and thermal stability of these four domains are analysed in relation to their global folds an evolutionary pattern emerges. Thus, in the evolution of novel binding properties mutations are allowed only as long as the energetically favourable global fold is maintained. | ||
Solution structure of the albumin-binding GA module: a versatile bacterial protein domain.,Johansson MU, de Chateau M, Wikstrom M, Forsen S, Drakenberg T, Bjorck L J Mol Biol. 1997 Mar 14;266(5):859-65. PMID:9086265<ref>PMID:9086265</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: Finegoldia magna]] | <div class="pdbe-citations 1gab" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Bjorck | <references/> | ||
[[Category: Chateau | __TOC__ | ||
[[Category: Drakenberg | </StructureSection> | ||
[[Category: Forsen | [[Category: Finegoldia magna ATCC 29328]] | ||
[[Category: Johansson | [[Category: Large Structures]] | ||
[[Category: Wikstrom | [[Category: Bjorck L]] | ||
[[Category: De Chateau M]] | |||
[[Category: Drakenberg T]] | |||
[[Category: Forsen S]] | |||
[[Category: Johansson MU]] | |||
[[Category: Wikstrom M]] | |||
Latest revision as of 11:31, 22 May 2024
STRUCTURE OF AN ALBUMIN-BINDING DOMAIN, NMR, 20 STRUCTURESSTRUCTURE OF AN ALBUMIN-BINDING DOMAIN, NMR, 20 STRUCTURES
Structural highlights
FunctionPAB_FINMA Binds serum albumin. 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 PubMedThe albumin-binding GA module is found in a family of surface proteins of different bacterial species. It comprises 45 amino acid residues and represents the first known example of contemporary module shuffling. Using 1H NMR spectroscopy we have determined the solution structure of the GA module from protein PAB, a protein of the anaerobic human commensal and pathogen Peptostreptococcus magnus. This structure, the first three-dimensional structure of an albumin-binding protein domain described, was shown to be composed of a left-handed three-helix-bundle. Sequence differences between GA modules with different affinities for albumin indicated that a conserved region in the C-terminal part of the second helix and the flexible sequence between helices 2 and 3 could contribute to the albumin-binding activity. The effect on backbone amide proton exchange rates upon binding to albumin support this assumption. The GA module has a fold that is strikingly similar to the immunoglobulin-binding domains of staphylococcal protein A but it shows no resemblance to the fold shared by the immunoglobulin-binding domains of streptococcal protein G and peptostreptococcal protein L. When the gene sequences, binding properties and thermal stability of these four domains are analysed in relation to their global folds an evolutionary pattern emerges. Thus, in the evolution of novel binding properties mutations are allowed only as long as the energetically favourable global fold is maintained. Solution structure of the albumin-binding GA module: a versatile bacterial protein domain.,Johansson MU, de Chateau M, Wikstrom M, Forsen S, Drakenberg T, Bjorck L J Mol Biol. 1997 Mar 14;266(5):859-65. PMID:9086265[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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