1tf0: Difference between revisions
New page: left|200px<br /> <applet load="1tf0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tf0, resolution 2.70Å" /> '''Crystal structure o... |
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[[Image:1tf0.gif|left|200px]]<br /> | [[Image:1tf0.gif|left|200px]]<br /><applet load="1tf0" size="350" color="white" frame="true" align="right" spinBox="true" | ||
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caption="1tf0, resolution 2.70Å" /> | caption="1tf0, resolution 2.70Å" /> | ||
'''Crystal structure of the GA module complexed with human serum albumin'''<br /> | '''Crystal structure of the GA module complexed with human serum albumin'''<br /> | ||
==Overview== | ==Overview== | ||
Many bactericide species express surface proteins that interact with human | Many bactericide species express surface proteins that interact with human serum albumin (HSA). Protein PAB from the anaerobic bacterium Finegoldia magna (formerly Peptostreptococcus magnus) represents one of these proteins. Protein PAB contains a domain of 53 amino acid residues known as the GA module. GA homologs are also found in protein G of group C and G streptococci. Here we report the crystal structure of HSA in complex with the GA module of protein PAB. The model of the complex was refined to a resolution of 2.7 A and reveals a novel binding epitope located in domain II of the albumin molecule. The GA module is composed of a left-handed three-helix bundle, and residues from the second helix and the loops surrounding it were found to be involved in HSA binding. Furthermore, the presence of HSA-bound fatty acids seems to influence HSA-GA complex formation. F. magna has a much more restricted host specificity compared with C and G streptococci, which is also reflected in the binding of different animal albumins by proteins PAB and G. The structure of the HSA-GA complex offers a molecular explanation to this unusually clear example of bacterial adaptation. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1TF0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with DKA and CIT as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 1TF0 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=DKA:'>DKA</scene> and <scene name='pdbligand=CIT:'>CIT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TF0 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Bjorck, L.]] | [[Category: Bjorck, L.]] | ||
[[Category: Frick, I | [[Category: Frick, I M.]] | ||
[[Category: Lejon, S.]] | [[Category: Lejon, S.]] | ||
[[Category: Svensson, S.]] | [[Category: Svensson, S.]] | ||
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[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:49 2008'' | ||
Revision as of 16:12, 21 February 2008
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Crystal structure of the GA module complexed with human serum albumin
OverviewOverview
Many bactericide species express surface proteins that interact with human serum albumin (HSA). Protein PAB from the anaerobic bacterium Finegoldia magna (formerly Peptostreptococcus magnus) represents one of these proteins. Protein PAB contains a domain of 53 amino acid residues known as the GA module. GA homologs are also found in protein G of group C and G streptococci. Here we report the crystal structure of HSA in complex with the GA module of protein PAB. The model of the complex was refined to a resolution of 2.7 A and reveals a novel binding epitope located in domain II of the albumin molecule. The GA module is composed of a left-handed three-helix bundle, and residues from the second helix and the loops surrounding it were found to be involved in HSA binding. Furthermore, the presence of HSA-bound fatty acids seems to influence HSA-GA complex formation. F. magna has a much more restricted host specificity compared with C and G streptococci, which is also reflected in the binding of different animal albumins by proteins PAB and G. The structure of the HSA-GA complex offers a molecular explanation to this unusually clear example of bacterial adaptation.
DiseaseDisease
Known diseases associated with this structure: Analbuminemia OMIM:[103600], Dysalbuminemic hyperthyroxinemia OMIM:[103600], Dysalbuminemic hyperzincemia OMIM:[103600]
About this StructureAbout this Structure
1TF0 is a Protein complex structure of sequences from Finegoldia magna and Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure and biological implications of a bacterial albumin binding module in complex with human serum albumin., Lejon S, Frick IM, Bjorck L, Wikstrom M, Svensson S, J Biol Chem. 2004 Oct 8;279(41):42924-8. Epub 2004 Jul 21. PMID:15269208
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