2Y5Q

Listeria monocytogenes InlB (internalin B) residues 36-392

Summary for 2Y5Q

• Entry DOI: 10.2210/pdb2y5q/pdb
• Related: 1D0B 1H6T 1M9S 1OTM 1OTN 1OTO 2UZX 2UZY 2WQU 2WQV 2WQW 2WQX 2Y5P
• Descriptor: INTERNALIN B, ZINC ION (2 entities in total)
• Functional Keywords: protein binding, leucine rich repeat, virulence factor, pathogenicity factor
• Biological source: LISTERIA MONOCYTOGENES
• Total number of polymer chains: 1
• Total formula weight: 40618.02

Authors

Ebbes, M.,Niemann, H.H. (deposition date: 2011-01-17, release date: 2011-02-23, Last modification date: 2023-12-20)

Primary citation

Ebbes, M.,Bleymuller, W.M.,Cernescu, M.,Nolker, R.,Brutschy, B.,Niemann, H.H.
Fold and Function of the Inlb B-Repeat.
J.Biol.Chem., 286:15496-, 2011

PubMed Abstract: Host cell invasion by the facultative intracellular pathogen Listeria monocytogenes requires the invasion protein InlB in many cell types. InlB consists of an N-terminal internalin domain that binds the host cell receptor tyrosine kinase Met and C-terminal GW domains that bind to glycosaminoglycans (GAGs). Met binding and activation is required for host cell invasion, while the interaction between GW domains and GAGs enhances this effect. Soluble InlB elicits the same cellular phenotypes as the natural Met ligand hepatocyte growth factor/scatter factor (HGF/SF), e.g. cell scatter. So far, little is known about the central part of InlB, the B-repeat. Here we present a structural and functional characterization of the InlB B-repeat. The crystal structure reveals a variation of the β-grasp fold that is most similar to small ubiquitin-like modifiers (SUMOs). However, structural similarity also suggests a potential evolutionary relation to bacterial mucin-binding proteins. The B-repeat defines the prototype structure of a hitherto uncharacterized domain present in over a thousand bacterial proteins. Generally, this domain probably acts as a spacer or a receptor-binding domain in extracellular multi-domain proteins. In cellular assays the B-repeat acts synergistically with the internalin domain conferring to it the ability to stimulate cell motility. Thus, the B-repeat probably binds a further host cell receptor and thereby enhances signaling downstream of Met.

PubMed: 21345802
DOI: 10.1074/JBC.M110.189951

Experimental method

X-RAY DIFFRACTION (3.2 Å)