1p9h

<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://proteopedia.org/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 "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://proteopedia.org/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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1p9h ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/YADA1_YEREN 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.<ref>PMID:2592347</ref>

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== 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<ref>PMID:14765110</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1p9h" style="background-color:#fffaf0;"></div>

[[Category: Bacterium enterocoliticum schleifstein and coleman 1939]]

[[Category: Goldman, A]]

[[Category: Merckel, M C]]

[[Category: Nummelin, H]]

[[Category: Skurnik, M]]

[[Category: Left-handed beta-roll]]