Adhesin: Difference between revisions
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**[[4k0o]], [[2bs8]] – EcF17b-G lectin domain – ''Escherichia coli'' <BR /> | **[[4k0o]], [[2bs8]] – EcF17b-G lectin domain – ''Escherichia coli'' <BR /> | ||
**[[4b4p]], [[4bwo]] – EcFedF lectin domain <BR /> | **[[4b4p]], [[4bwo]] – EcFedF lectin domain <BR /> | ||
**[[1psz]] – SpPsaA + Zn – ''Streptococcus pneumonia''<br /> | **[[1psz]] – SpPsaA + Zn – ''Streptococcus pneumonia''<br /> | ||
**[[3ztt]] – SpPsaA + Mn<br /> | **[[3ztt]] – SpPsaA + Mn<br /> | ||
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**[[3zk7]] – SpPsaA <br /> | **[[3zk7]] – SpPsaA <br /> | ||
**[[3zk8]], [[3zk9]], [[3zka]] – SpPsaA (mutant)<br /> | **[[3zk8]], [[3zk9]], [[3zka]] – SpPsaA (mutant)<br /> | ||
**[[5cyl]] – PsaA subunit CUPB6 - ''Pseudomonas aeruginosa''<br /> | |||
* Fimbrial adhesion complex | |||
**[[2bs7]] – EcF17b-G lectin domain + chitobiose <BR /> | **[[2bs7]] – EcF17b-G lectin domain + chitobiose <BR /> | ||
**[[3ffo]] – EcF17b-G lectin domain + GlcNac-Man <BR /> | **[[3ffo]] – EcF17b-G lectin domain + GlcNac-Man <BR /> | ||
**[[4b4q]], [[4b4r]] – EcFedF lectin domain + hexasaccharide <BR /> | |||
**[[4w6w]], [[4w6x]], [[4w6y]] – EcFedF lectin domain + nanobody <BR /> | |||
**[[4f8l]] – YpPsaA + galactose + inhibitor – ''Yersinia pestis'' <BR /> | **[[4f8l]] – YpPsaA + galactose + inhibitor – ''Yersinia pestis'' <BR /> | ||
**[[4f8n]] – YpPsaA + galactose + phosphate choline <BR /> | **[[4f8n]] – YpPsaA + galactose + phosphate choline <BR /> | ||
Revision as of 22:20, 1 November 2016
FunctionAdhesins (Adh) are surface components of bacteria which facillitate adhesion to surfaces or other cells. Adh are specific surface recognition protein and are regarded as virulence factors.[1] For trimeric autotransporter adhesin see EibD. DiseaseBacterial pathogens use adhesins as a major factor in adhesion-based virulence. Adhesins serve as vaccine targets since they are essential to infection.
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3D Structures of adhesin3D Structures of adhesin
Updated on 01-November-2016
ReferencesReferences
- ↑ Klemm P, Schembri MA. Bacterial adhesins: function and structure. Int J Med Microbiol. 2000 Mar;290(1):27-35. PMID:11043979 doi:http://dx.doi.org/10.1016/S1438-4221(00)80102-2
- ↑ Bao R, Nair MK, Tang WK, Esser L, Sadhukhan A, Holland RL, Xia D, Schifferli DM. Structural basis for the specific recognition of dual receptors by the homopolymeric pH 6 antigen (Psa) fimbriae of Yersinia pestis. Proc Natl Acad Sci U S A. 2013 Jan 15;110(3):1065-70. doi:, 10.1073/pnas.1212431110. Epub 2012 Dec 31. PMID:23277582 doi:10.1073/pnas.1212431110