2ylh

From Proteopedia

(Difference between revisions)

Current revision

Structure of N-terminal domain of Candida albicans Als9-2 G299W mutant

Structural highlights

2ylh is a 1 chain structure with sequence from Candida albicans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.7Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ALS9_CANAL Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections (PubMed:17510860, PubMed:22321066, PubMed:22429754). Allele ALS9-2 contributes to endothelial cell adhesion, whereas ALS9-1 does not (PubMed:17600078).^[1] ^[2] ^[3] ^[4]

Publication Abstract from PubMed

Candida albicans is the most prevalent fungal pathogen in humans and a major source of life-threatening nosocomial infections. The Als (agglutinin-like sequence) glycoproteins are an important virulence factor for this fungus and have been associated with binding of host-cell surface proteins and small peptides of random sequence, the formation of biofilms and amyloid fibers. High-resolution structures of N-terminal Als adhesins (NT-Als; up to 314 amino acids) show that ligand recognition relies on a motif capable of binding flexible C termini of peptides in extended conformation. Central to this mechanism is an invariant lysine that recognizes the C-terminal carboxylate of ligands at the end of a deep-binding cavity. In addition to several protein-peptide interactions, a network of water molecules runs parallel to one side of the ligand and contributes to the recognition of diverse peptide sequences. These data establish NT-Als adhesins as a separate family of peptide-binding proteins and an unexpected adhesion system for primary, widespread protein-protein interactions at the Candida/host-cell interface.

Structural basis for the broad specificity to host-cell ligands by the pathogenic fungus Candida albicans.,Salgado PS, Yan R, Taylor JD, Burchell L, Jones R, Hoyer LL, Matthews SJ, Simpson PJ, Cota E Proc Natl Acad Sci U S A. 2011 Sep 20;108(38):15775-9. Epub 2011 Sep 6. PMID:21896717^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Klotz SA, Gaur NK, De Armond R, Sheppard D, Khardori N, Edwards JE Jr, Lipke PN, El-Azizi M. Candida albicans Als proteins mediate aggregation with bacteria and yeasts. Med Mycol. 2007 Jun;45(4):363-70. doi: 10.1080/13693780701299333. PMID:17510860 doi:http://dx.doi.org/10.1080/13693780701299333
↑ Zhao X, Oh SH, Hoyer LL. Unequal contribution of ALS9 alleles to adhesion between Candida albicans and human vascular endothelial cells. Microbiology (Reading). 2007 Jul;153(Pt 7):2342-2350. doi:, 10.1099/mic.0.2006/005017-0. PMID:17600078 doi:http://dx.doi.org/10.1099/mic.0.2006/005017-0
↑ Aoki W, Kitahara N, Miura N, Morisaka H, Kuroda K, Ueda M. Profiling of adhesive properties of the agglutinin-like sequence (ALS) protein family, a virulent attribute of Candida albicans. FEMS Immunol Med Microbiol. 2012 Jun;65(1):121-4. doi:, 10.1111/j.1574-695X.2012.00941.x. Epub 2012 Mar 6. PMID:22321066 doi:http://dx.doi.org/10.1111/j.1574-695X.2012.00941.x
↑ Monroy-Perez E, Sainz-Espunes T, Paniagua-Contreras G, Negrete-Abascal E, Rodriguez-Moctezuma JR, Vaca S. Frequency and expression of ALS and HWP1 genotypes in Candida albicans strains isolated from Mexican patients suffering from vaginal candidosis. Mycoses. 2012 May;55(3):e151-7. doi: 10.1111/j.1439-0507.2012.02188.x. Epub 2012 , Mar 19. PMID:22429754 doi:http://dx.doi.org/10.1111/j.1439-0507.2012.02188.x
↑ Salgado PS, Yan R, Taylor JD, Burchell L, Jones R, Hoyer LL, Matthews SJ, Simpson PJ, Cota E. Structural basis for the broad specificity to host-cell ligands by the pathogenic fungus Candida albicans. Proc Natl Acad Sci U S A. 2011 Sep 20;108(38):15775-9. Epub 2011 Sep 6. PMID:21896717 doi:10.1073/pnas.1103496108

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ylh"

Categories: Candida albicans | Large Structures | Burchell L | Cota E | Salgado PS

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 2ylh is ON HOLD  until Paper Publication
+==Structure of N-terminal domain of Candida albicans Als9-2 G299W mutant==
+<StructureSection load='2ylh' size='340' side='right'caption='[[2ylh]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[2ylh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans Candida albicans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YLH FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=2ylh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ylh OCA], [https://pdbe.org/2ylh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ylh RCSB], [https://www.ebi.ac.uk/pdbsum/2ylh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ylh ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ALS9_CANAL ALS9_CANAL] Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections (PubMed:17510860, PubMed:22321066, PubMed:22429754). Allele ALS9-2 contributes to endothelial cell adhesion, whereas ALS9-1 does not (PubMed:17600078).<ref>PMID:17510860</ref> <ref>PMID:17600078</ref> <ref>PMID:22321066</ref> <ref>PMID:22429754</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Candida albicans is the most prevalent fungal pathogen in humans and a major source of life-threatening nosocomial infections. The Als (agglutinin-like sequence) glycoproteins are an important virulence factor for this fungus and have been associated with binding of host-cell surface proteins and small peptides of random sequence, the formation of biofilms and amyloid fibers. High-resolution structures of N-terminal Als adhesins (NT-Als; up to 314 amino acids) show that ligand recognition relies on a motif capable of binding flexible C termini of peptides in extended conformation. Central to this mechanism is an invariant lysine that recognizes the C-terminal carboxylate of ligands at the end of a deep-binding cavity. In addition to several protein-peptide interactions, a network of water molecules runs parallel to one side of the ligand and contributes to the recognition of diverse peptide sequences. These data establish NT-Als adhesins as a separate family of peptide-binding proteins and an unexpected adhesion system for primary, widespread protein-protein interactions at the Candida/host-cell interface.
-Authors: Salgado, P.S., Burchell, L., Cota, E.
+Structural basis for the broad specificity to host-cell ligands by the pathogenic fungus Candida albicans.,Salgado PS, Yan R, Taylor JD, Burchell L, Jones R, Hoyer LL, Matthews SJ, Simpson PJ, Cota E Proc Natl Acad Sci U S A. 2011 Sep 20;108(38):15775-9. Epub 2011 Sep 6. PMID:21896717<ref>PMID:21896717</ref>
-Description: Structure of N-terminal domain of Candida albicans Als9-2 G299W mutant
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2ylh" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Candida albicans]]
+[[Category: Large Structures]]
+[[Category: Burchell L]]
+[[Category: Cota E]]
+[[Category: Salgado PS]]

2ylh

From Proteopedia

Current revision

Structure of N-terminal domain of Candida albicans Als9-2 G299W mutant

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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