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New page: left|200px<br /><applet load="1gjt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gjt" /> '''SOLUTION STRUCTURE OF THE ALBUMIN BINDING DO... |
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== | ==Solution structure of the Albumin binding domain of Streptococcal Protein G== | ||
We have determined the solution structure of an albumin binding domain of | <StructureSection load='1gjt' size='340' side='right'caption='[[1gjt]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1gjt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp._'group_G' Streptococcus sp. 'group G']. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GJT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1GJT 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=1gjt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gjt OCA], [https://pdbe.org/1gjt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1gjt RCSB], [https://www.ebi.ac.uk/pdbsum/1gjt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1gjt ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SPG2_STRSG SPG2_STRSG] | |||
== 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/gj/1gjt_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=1gjt ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
We have determined the solution structure of an albumin binding domain of protein G, a surface protein of group C and G streptococci. We find that it folds into a left handed three-helix bundle similar to the albumin binding domain of protein PAB from Peptostreptococcus magnus. The two domains share 59% sequence identity, are thermally very stable, and bind to the same site on human serum albumin. The albumin binding site, the first determined for this structural motif known as the GA module, comprises residues spanning the first loop to the beginning of the third helix and includes the most conserved region of GA modules. The two GA modules have different affinities for albumin from different species, and their albumin binding patterns correspond directly to the host specificity of C/G streptococci and P. magnus, respectively. These studies of the evolution, structure, and binding properties of the GA module emphasize the power of bacterial adaptation and underline ecological and medical problems connected with the use of antibiotics. | |||
Structure, specificity, and mode of interaction for bacterial albumin-binding modules.,Johansson MU, Frick IM, Nilsson H, Kraulis PJ, Hober S, Jonasson P, Linhult M, Nygren PA, Uhlen M, Bjorck L, Drakenberg T, Forsen S, Wikstrom M J Biol Chem. 2002 Mar 8;277(10):8114-20. Epub 2001 Dec 18. PMID:11751858<ref>PMID:11751858</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1gjt" style="background-color:#fffaf0;"></div> | ||
[[Category: Streptococcus sp. group | == References == | ||
[[Category: Bjorck | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: Frick | </StructureSection> | ||
[[Category: Hober | [[Category: Large Structures]] | ||
[[Category: Johansson | [[Category: Streptococcus sp. 'group G']] | ||
[[Category: Jonasson | [[Category: Bjorck L]] | ||
[[Category: Kraulis | [[Category: Drakenberg T]] | ||
[[Category: Nilsson | [[Category: Forsen S]] | ||
[[Category: Nygren | [[Category: Frick IM]] | ||
[[Category: Uhlen | [[Category: Hober S]] | ||
[[Category: Wikstrom | [[Category: Johansson MU]] | ||
[[Category: Jonasson P]] | |||
[[Category: Kraulis PJ]] | |||
[[Category: Nilsson H]] | |||
[[Category: Nygren AP]] | |||
[[Category: Uhlen M]] | |||
[[Category: Wikstrom M]] | |||
Latest revision as of 08:30, 15 May 2024
Solution structure of the Albumin binding domain of Streptococcal Protein GSolution structure of the Albumin binding domain of Streptococcal Protein G
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedWe have determined the solution structure of an albumin binding domain of protein G, a surface protein of group C and G streptococci. We find that it folds into a left handed three-helix bundle similar to the albumin binding domain of protein PAB from Peptostreptococcus magnus. The two domains share 59% sequence identity, are thermally very stable, and bind to the same site on human serum albumin. The albumin binding site, the first determined for this structural motif known as the GA module, comprises residues spanning the first loop to the beginning of the third helix and includes the most conserved region of GA modules. The two GA modules have different affinities for albumin from different species, and their albumin binding patterns correspond directly to the host specificity of C/G streptococci and P. magnus, respectively. These studies of the evolution, structure, and binding properties of the GA module emphasize the power of bacterial adaptation and underline ecological and medical problems connected with the use of antibiotics. Structure, specificity, and mode of interaction for bacterial albumin-binding modules.,Johansson MU, Frick IM, Nilsson H, Kraulis PJ, Hober S, Jonasson P, Linhult M, Nygren PA, Uhlen M, Bjorck L, Drakenberg T, Forsen S, Wikstrom M J Biol Chem. 2002 Mar 8;277(10):8114-20. Epub 2001 Dec 18. PMID:11751858[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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