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1p9h

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Revision as of 01:36, 11 September 2015

CRYSTAL STRUCTURE OF THE COLLAGEN-BINDING DOMAIN OF YERSINIA ADHESIN YadA

Structural highlights

1p9h is a 1 chain structure with sequence from "bacterium_enterocoliticum"_schleifstein_and_coleman_1939 "bacterium enterocoliticum" schleifstein and coleman 1939. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	YADA OR YOPA OR INVA OR YOP1 ("Bacterium enterocoliticum" Schleifstein and Coleman 1939)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[YADA1_YEREN] Collagen-binding outer membrane protein forming a fibrillar matrix on the bacterial cell surface. Promotes initial attachment and invasion of eukaryotic cells. Also protects the bacteria by being responsible for agglutination, serum resistance, complement inactivation and phagocytosis resistance.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of the recombinant collagen-binding domain of Yersinia adhesin YadA from Yersinia enterocolitica serotype O:3 was solved at 1.55 A resolution. The trimeric structure is composed of head and neck regions, and the collagen binding head region is a novel nine-coiled left-handed parallel beta-roll. Before the beta-roll, the polypeptide loops from one monomer to the rest, and after the beta-roll the neck region does the same, making the transition from the globular head region to the narrower stalk domain. This creates an intrinsically stable 'lock nut' structure. The trimeric form of YadA is required for collagen binding, and mutagenesis of its surface residues allowed identification of a putative collagen-binding surface. Furthermore, a new structure-sequence motif for YadA beta-roll was used to identify putative YadA-head-like domains in a variety of human and plant pathogens. Such domains may therefore be a common bacterial strategy for avoiding host response.

The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll.,Nummelin H, Merckel MC, Leo JC, Lankinen H, Skurnik M, Goldman A EMBO J. 2004 Feb 25;23(4):701-11. Epub 2004 Feb 5. PMID:14765110^[2]

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

References

↑ Emody L, Heesemann J, Wolf-Watz H, Skurnik M, Kapperud G, O'Toole P, Wadstrom T. Binding to collagen by Yersinia enterocolitica and Yersinia pseudotuberculosis: evidence for yopA-mediated and chromosomally encoded mechanisms. J Bacteriol. 1989 Dec;171(12):6674-9. PMID:2592347
↑ Nummelin H, Merckel MC, Leo JC, Lankinen H, Skurnik M, Goldman A. The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll. EMBO J. 2004 Feb 25;23(4):701-11. Epub 2004 Feb 5. PMID:14765110 doi:10.1038/sj.emboj.7600100

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1p9h"

@@ Line 2: / Line 2: @@
 <StructureSection load='1p9h' size='340' side='right' caption='[[1p9h]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1p9h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Yersinia_enterocolitica Yersinia enterocolitica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P9H FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1p9h]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_enterocoliticum"_schleifstein_and_coleman_1939 "bacterium enterocoliticum" schleifstein and coleman 1939]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P9H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1P9H FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YADA OR YOPA OR INVA OR YOP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=630 Yersinia enterocolitica])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YADA OR YOPA OR INVA OR YOP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=630 "Bacterium enterocoliticum" Schleifstein and Coleman 1939])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p9h OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1p9h RCSB], [http://www.ebi.ac.uk/pdbsum/1p9h PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1p9h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p9h OCA], [http://pdbe.org/1p9h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1p9h RCSB], [http://www.ebi.ac.uk/pdbsum/1p9h PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1p9h" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Adhesin|Adhesin]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Yersinia enterocolitica]]
+[[Category: Bacterium enterocoliticum schleifstein and coleman 1939]]
 [[Category: Goldman, A]]
 [[Category: Merckel, M C]]

1p9h

From Proteopedia

Revision as of 01:36, 11 September 2015

CRYSTAL STRUCTURE OF THE COLLAGEN-BINDING DOMAIN OF YERSINIA ADHESIN YadA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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