Adhesin
From Proteopedia
(Difference between revisions)
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*Fimbrial adhesin | *Fimbrial adhesin | ||
| - | **[[4k0o]], [[2bs8]], [[2bsc]], [[2bsb]] – EcF17b-G lectin domain – ''Escherichia coli'' <BR /> | + | **[[4k0o]], [[2bs8]], [[2bsc]], [[2bsb]], [[5nwp]] – EcF17b-G lectin domain – ''Escherichia coli'' <BR /> |
| - | **[[ | + | **[[1o9z]], [[1o9w]], [[1o9v]] – EcF17a-G lectin domain <BR /> |
| - | **[[ | + | **[[5vq5]] – EcF17 lectin domain (mutant) <BR /> |
| - | **[[ | + | **[[1oio]] – EcF17c lectin domain <BR /> |
| + | **[[4b4p]], [[4bwo]] – EcF18 lectin domain <BR /> | ||
| + | **[[4auu]], [[1uwf]], [[1tr7]], [[5fwr]] – EcAdh FimH lectin domain <BR /> | ||
| + | **[[5mca]], [[5fx3]] – EcAdh FimH lectin domain (mutant) <BR /> | ||
**[[5afo]] – EcAdh LF82 <BR /> | **[[5afo]] – EcAdh LF82 <BR /> | ||
| - | **[[ | + | **[[6aow]] – EcAdh FMLH lectin domain <BR /> |
| - | + | **[[3zk7]] – SpPsaA - ''Streptococcus pneumoniae'' <br /> | |
| - | + | ||
| - | + | ||
| - | **[[ | + | |
| - | + | ||
| - | + | ||
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**[[3zk8]], [[3zk9]], [[3zka]] – SpPsaA (mutant)<br /> | **[[3zk8]], [[3zk9]], [[3zka]] – SpPsaA (mutant)<br /> | ||
| - | **[[ | + | **[[3u4k]] – Adh lectin domain – ''Klebsiella pneumoniae''<BR /> |
| - | * Fimbrial adhesion | + | *Fimbrial adhesion complexes |
| + | **[[4b4q]], [[4b4r]] – EcF18 lectin domain + hexasaccharide <BR /> | ||
| + | **[[4w6w]], [[4w6x]], [[4w6y]] – EcF18 lectin domain + nanobody <BR /> | ||
| + | **[[4j3o]] – EcAdh FimH + FimG + FimC + FimF + FimD <BR /> | ||
| + | **[[3rfz]], [[1ze3]] – EcAdh FimH + FimC + FimD <BR /> | ||
| + | **[[1qun]], [[1klf]], [[1kiu]] – EcAdh FimH + FimC <BR /> | ||
| + | **[[4xo9]] – EcAdh FimH + DSG residues 24-37 <BR /> | ||
| + | **[[4xod]], [[4xoa]] – EcAdh FimH + FimG residues 24-37 <BR /> | ||
| + | **[[4xob]] – EcAdh FimH + FimF residues 24-37 + mannoside derivative<BR /> | ||
| + | **[[5jr4]], [[5jqi]] – EcAdh FimH (mutant) + FimG N-terminal <BR /> | ||
| + | **[[6as8]], [[6arm]], [[6aoy]] – EcAdh FMLD lectin domain + galactoside derivative <BR /> | ||
| + | **[[6aox]] – EcAdh FMLD lectin domain + TF antigen <BR /> | ||
| + | **[[6aro]] – EcAdh FMLH lectin domain + quinoline derivative <BR /> | ||
| + | **[[5muc]], [[5l4y]], [[5l4x]], [[5l4w]], [[5l4v]], [[5l4u]], [[5l4t]], [[5jcq]], [[5jcr]], [[5f2f]], [[5f3f]], [[5abz]], [[4xo8]], [[4x5p]], [[4x5q]], [[4x5r]], [[4lov]], [[4css]], [[4cst]], [[4att]], [[4auj]], [[4auy]], [[4av0]], [[4av4]], [[4av5]], [[4avh]], [[4avi]], [[4avj]], [[4avk]], [[3zl1]], [[3zl2]], [[2vco]] – EcAdh FimH lectin domain + mannoside derivative <BR /> | ||
| + | **[[5cgb]] – EcAdh FimH lectin domain + galactitol <BR /> | ||
| + | **[[5ab1]], [[4x50]] – EcAdh FimH + mannoside derivative <BR /> | ||
| + | **[[5aap]], [[5aal]], [[5mts]] – EcAdh FimH lectin domain + anti-adhesive <BR /> | ||
| + | **[[3f6j]], [[3f64]], [[1zpl]], [[1zk5]] – EcF17a-G lectin domain + GlcNAc derivative <BR /> | ||
| + | |||
| + | |||
| + | **[[1psz]] – SpPsaA + Zn – ''Streptococcus pneumonia''<br /> | ||
| + | **[[3ztt]] – SpPsaA + Mn<br /> | ||
| + | **[[4utp]], [[4uto]] – SpPsaA + Cd<br /> | ||
**[[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 /> | ||
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**[[3lt6]], [[3lt7]] – YeYadA coiled coil<br /> | **[[3lt6]], [[3lt7]] – YeYadA coiled coil<br /> | ||
**[[2lme]] – YeYadA coiled coil - NMR<br /> | **[[2lme]] – YeYadA coiled coil - NMR<br /> | ||
| + | |||
| + | *Serine-rich adhesin for platelets (SRAP) | ||
| + | |||
| + | **[[4m00]] – SaSRAP LBD<br /> | ||
| + | **[[4m01]] – SaSRAP LBD N-terminal<br /> | ||
| + | **[[4m02]] – SaSRAP LBD middle region<br /> | ||
| + | **[[4m03]] – SaSRAP LBD C-terminal<br /> | ||
*Adhesin | *Adhesin | ||
| - | **[[2odl]], [[2gr8]], [[2gr7]] – | + | **[[2odl]], [[2gr8]], [[2gr7]] – HiAdh secretion domain – ''Haemophilus influenzae''<br /> |
| + | **[[3emf]] – HiAdh residues 51-166<br /> | ||
| + | **[[3emi]] – HiAdh residues 307-422 (mutant)<br /> | ||
| + | **[[1s7m]] – HiAdh residues 548-706<br /> | ||
| + | **[[3emo]] – HiAdh residues 937-1098<br /> | ||
**[[4zh7]], [[4zh0]] – Adh BABA – ''Helicobacter pylori''<br /> | **[[4zh7]], [[4zh0]] – Adh BABA – ''Helicobacter pylori''<br /> | ||
**[[4usx]] – Adh trimeric autotransporter – ''Burkholderia pseudomallei''<br /> | **[[4usx]] – Adh trimeric autotransporter – ''Burkholderia pseudomallei''<br /> | ||
**[[3wqa]], [[3wpr]], [[3wpp]], [[3wpo]], [[3wpa]] – AcAdh trimeric autotransporter C-terminal – ''Acinetobacter''<br /> | **[[3wqa]], [[3wpr]], [[3wpp]], [[3wpo]], [[3wpa]] – AcAdh trimeric autotransporter C-terminal – ''Acinetobacter''<br /> | ||
**[[3wp8]] – AcAdh trimeric autotransporter C-terminal (mutant)<br /> | **[[3wp8]] – AcAdh trimeric autotransporter C-terminal (mutant)<br /> | ||
| + | **[[4err]] – Adh autotransporter effector domain – ''Vibrio vulnificus''<br /> | ||
| + | **[[2wps]], [[2wpr]], [[2wpq]] – Adh trimeric autotransporter residues 483-523 – ''Salmonella enterica''<br /> | ||
**[[4tsh]] – Adh surface protein – ''Streptococcus mutans''<br /> | **[[4tsh]] – Adh surface protein – ''Streptococcus mutans''<br /> | ||
**[[4mee]] – EcAdh diffuse adherence C-terminal <br /> | **[[4mee]] – EcAdh diffuse adherence C-terminal <br /> | ||
| + | **[[5lvy]] – EcAdh lectin domain <BR /> | ||
**[[3etw]] – FnAdh A – ''Fusobacterium nucleatum'' <BR /> | **[[3etw]] – FnAdh A – ''Fusobacterium nucleatum'' <BR /> | ||
| - | **[[3etz]], [[3ety]], [[3etx]] – FnAdh A (mutant) <BR /> | + | **[[3etz]], [[3ety]], [[3etx]], [[2gl2]] – FnAdh A (mutant) <BR /> |
**[[3d9x]] – Adh A – ''Bartonella henselae'' <BR /> | **[[3d9x]] – Adh A – ''Bartonella henselae'' <BR /> | ||
**[[2lwb]] – Adh WI-1 – ''Ajellomyces dermatitidis'' <BR /> | **[[2lwb]] – Adh WI-1 – ''Ajellomyces dermatitidis'' <BR /> | ||
| - | + | **[[5my7]] – Adh – ''Neisseria meningitidis'' <BR /> | |
}} | }} | ||
Revision as of 09:12, 8 March 2018
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3D Structures of adhesin
Updated on 08-March-2018
References
- ↑ 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
- ↑ Nishiyama M, Ishikawa T, Rechsteiner H, Glockshuber R. Reconstitution of pilus assembly reveals a bacterial outer membrane catalyst. Science. 2008 Apr 18;320(5874):376-9. doi: 10.1126/science.1154994. Epub 2008 Mar, 27. PMID:18369105 doi:http://dx.doi.org/10.1126/science.1154994
- ↑ Wizemann TM, Adamou JE, Langermann S. Adhesins as targets for vaccine development. Emerg Infect Dis. 1999 May-Jun;5(3):395-403. doi: 10.3201/eid0503.990310. PMID:10341176 doi:http://dx.doi.org/10.3201/eid0503.990310
- ↑ 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

