1gab: Difference between revisions

New page: left|200px<br /><applet load="1gab" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gab" /> '''STRUCTURE OF AN ALBUMIN-BINDING DOMAIN, NMR,...
 
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[[Image:1gab.gif|left|200px]]<br /><applet load="1gab" size="450" color="white" frame="true" align="right" spinBox="true"
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'''STRUCTURE OF AN ALBUMIN-BINDING DOMAIN, NMR, 20 STRUCTURES'''<br />


==Overview==
==STRUCTURE OF AN ALBUMIN-BINDING DOMAIN, NMR, 20 STRUCTURES==
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.
<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.


==About this Structure==
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>
1GAB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1GAB OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9086265 9086265]
</div>
[[Category: Finegoldia magna]]
<div class="pdbe-citations 1gab" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
== References ==
[[Category: Bjorck, L.]]
<references/>
[[Category: Chateau, M.De.]]
__TOC__
[[Category: Drakenberg, T.]]
</StructureSection>
[[Category: Forsen, S.]]
[[Category: Finegoldia magna ATCC 29328]]
[[Category: Johansson, M.U.]]
[[Category: Large Structures]]
[[Category: Wikstrom, M.]]
[[Category: Bjorck L]]
[[Category: albumin-binding protein]]
[[Category: De Chateau M]]
[[Category: bacterial surface proteins]]
[[Category: Drakenberg T]]
[[Category: evolution]]
[[Category: Forsen S]]
[[Category: module shuffling]]
[[Category: Johansson MU]]
 
[[Category: Wikstrom M]]
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