{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,17]],"date-time":"2026-10-17T02:53:39Z","timestamp":1792205619936,"version":"4.4.0"},"reference-count":38,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2012,9,18]],"date-time":"2012-09-18T00:00:00Z","timestamp":1347926400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecular Microbiology"],"published-print":{"date-parts":[[2012,11]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p><jats:italic><jats:styled-content style=\"fixed-case\">K<\/jats:styled-content>lebsiella<\/jats:italic> species are members of the family enterobacteriaceae, opportunistic pathogens that are among the eight most prevalent infectious agents in hospitals. Among other virulence factors in <jats:italic><jats:styled-content style=\"fixed-case\">K<\/jats:styled-content>lebsiella<\/jats:italic>, type 3 pili exhibit a unique binding pattern in the human kidney via interaction of two <jats:styled-content style=\"fixed-case\">MrkD<\/jats:styled-content> adhesion variants 1<jats:styled-content style=\"fixed-case\">C<\/jats:styled-content>1 and 1<jats:styled-content style=\"fixed-case\">P<\/jats:styled-content> to type <jats:styled-content style=\"fixed-case\">IV<\/jats:styled-content> and\/or <jats:styled-content style=\"fixed-case\">V<\/jats:styled-content> collagen. However, very little is known about the nature of this recognition. Here we present the crystal structure of the plasmid born <jats:styled-content style=\"fixed-case\">MrkD<jats:sub>1P<\/jats:sub><\/jats:styled-content> receptor domain (<jats:styled-content style=\"fixed-case\">MrkDrd<\/jats:styled-content>). The structure reveals a jelly\u2010roll \u03b2\u2010barrel fold comprising 17 \u03b2\u2010strands very similar to the receptor domain of <jats:styled-content style=\"fixed-case\">GafD<\/jats:styled-content>, the tip adhesin from the <jats:styled-content style=\"fixed-case\">F<\/jats:styled-content>17 pilus that recognizes <jats:sc>n<\/jats:sc>\u2010acetyl\u2010<jats:sc>d<\/jats:sc>\u2010glucosamine (<jats:styled-content style=\"fixed-case\">GlcNAc<\/jats:styled-content>). Analysis of collagen <jats:styled-content style=\"fixed-case\">V<\/jats:styled-content> binding of different <jats:styled-content style=\"fixed-case\">MrkD<jats:sub>1P<\/jats:sub><\/jats:styled-content> mutants revealed that two regions were responsible for its binding: a pocket, that aligns approximately with the <jats:styled-content style=\"fixed-case\">GlcNAc<\/jats:styled-content> binding pocket of <jats:styled-content style=\"fixed-case\">GafD<\/jats:styled-content> involving residues <jats:styled-content style=\"fixed-case\">R<\/jats:styled-content>105 and <jats:styled-content style=\"fixed-case\">Y<\/jats:styled-content>155, and a transversally oriented patch that spans strands \u03b22a, \u03b29b and \u03b26 including residues <jats:styled-content style=\"fixed-case\">V<\/jats:styled-content>49, <jats:styled-content style=\"fixed-case\">T<\/jats:styled-content>52, <jats:styled-content style=\"fixed-case\">V<\/jats:styled-content>91, <jats:styled-content style=\"fixed-case\">R<\/jats:styled-content>102 and <jats:styled-content style=\"fixed-case\">I<\/jats:styled-content>136. Taken together, these data provide structural and functional insights on <jats:styled-content style=\"fixed-case\">MrkD<jats:sub>1P<\/jats:sub><\/jats:styled-content> recognition of host cells, providing a tool for future development of rationally designed drugs with the prospect of blocking <jats:italic><jats:styled-content style=\"fixed-case\">K<\/jats:styled-content>lebsiella<\/jats:italic> adhesion to collagen <jats:styled-content style=\"fixed-case\">V<\/jats:styled-content>.<\/jats:p>","DOI":"10.1111\/mmi.12023","type":"journal-article","created":{"date-parts":[[2012,9,19]],"date-time":"2012-09-19T04:20:44Z","timestamp":1348028444000},"page":"882-893","source":"Crossref","is-referenced-by-count":26,"title":["Crystal structure of the <scp>MrkD<sub>1P<\/sub><\/scp> receptor binding domain of <i><scp>K<\/scp>lebsiella pneumoniae<\/i> and identification of the human collagen <scp>V<\/scp> binding interface"],"prefix":"10.1111","volume":"86","author":[{"given":"Ana Toste","family":"R\u00eago","sequence":"first","affiliation":[{"name":"Institute of Structural and Molecular Biology University College London and Birkbeck College  Malet Street London WC1E\u20097HX UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jeremiah G.","family":"Johnson","sequence":"additional","affiliation":[{"name":"Department of Microbiology College of Medicine University of Iowa  Iowa City Iowa 52242 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sebastian","family":"Geibel","sequence":"additional","affiliation":[{"name":"Institute of Structural and Molecular Biology University College London and Birkbeck College  Malet Street London WC1E\u20097HX UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francisco J.","family":"Enguita","sequence":"additional","affiliation":[{"name":"Instituto de Medicina Molecular Faculdade de Medicina Universidade de Lisboa  Lisboa Portugal"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven","family":"Clegg","sequence":"additional","affiliation":[{"name":"Department of Microbiology College of Medicine University of Iowa  Iowa City Iowa 52242 USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gabriel","family":"Waksman","sequence":"additional","affiliation":[{"name":"Institute of Structural and Molecular Biology University College London and Birkbeck College  Malet Street London WC1E\u20097HX UK"},{"name":"Research Department of Structural and Molecular Biology University College London  Gower Street WC1E\u20096BT 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