EibD: Difference between revisions

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<scene name='EibD/2xqh/1'>Asymmetric unit</scene> contains a single polypeptide chain. The <scene name='EibD/2xqh_ba/3'>biological assembly</scene> consists of three copies of the monomer related by a three fold axis.
<scene name='EibD/2xqh/1'>Asymmetric unit</scene> contains a single polypeptide chain. The <scene name='EibD/2xqh_ba/3'>biological assembly</scene> consists of three copies of the monomer related by a three fold axis.
There are five distinct domains:
There are five distinct domains:
- YadA-like β-roll domain (ref);
- YadA-like β-roll domain (ref);<br>
- neck domain;
- neck domain;<br>
- right handed coiled-coil domain;
- right handed coiled-coil domain;<br>
- mini β-sheet domain;
- mini β-sheet domain;<br>
- left handed coiled-coil domain;
- left handed coiled-coil domain;<br>





Revision as of 12:09, 6 September 2012

Crystal structure of an immunoglobulin-binding fragment of the trimeric autotransporter adhesin (TAA) EibD

Crystal structure of an immunoglobulin-binding fragment of the trimeric autotransporter adhesin (TAA) EibD (PDB entry 2xqh)

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Primery reference

  1. Leo JC, Lyskowski A, Hattula K, Hartmann MD, Schwarz H, Butcher SJ, Linke D, Lupas AN, Goldman A. The Structure of E. coli IgG-Binding Protein D Suggests a General Model for Bending and Binding in Trimeric Autotransporter Adhesins. Structure. 2011 Jul 13;19(7):1021-30. PMID:21742268 doi:10.1016/j.str.2011.03.021

Proteopedia Page Contributors and Editors (what is this?)

Andrzej Lyskowski, Michal Harel