PMID- 21345802
OWN - NLM
STAT- MEDLINE
DCOM- 20110714
LR  - 20211020
IS  - 1083-351X (Electronic)
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 286
IP  - 17
DP  - 2011 Apr 29
TI  - Fold and function of the InlB B-repeat.
PG  - 15496-506
LID - 10.1074/jbc.M110.189951 [doi]
AB  - 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 beta-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.
FAU - Ebbes, Maria
AU  - Ebbes M
AD  - Department of Chemistry, Bielefeld University, Universitatsstrasse 25, 33615 
      Bielefeld, Germany.
FAU - Bleymuller, Willem M
AU  - Bleymuller WM
FAU - Cernescu, Mihaela
AU  - Cernescu M
FAU - Nolker, Rolf
AU  - Nolker R
FAU - Brutschy, Bernd
AU  - Brutschy B
FAU - Niemann, Hartmut H
AU  - Niemann HH
LA  - eng
SI  - PDB/2Y5P
SI  - PDB/2Y5Q
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20110223
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Bacterial Proteins)
RN  - 0 (Membrane Proteins)
RN  - EC 2.7.10.1 (Proto-Oncogene Proteins c-met)
RN  - EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases)
SB  - IM
MH  - Animals
MH  - Bacterial Proteins/*chemistry/metabolism
MH  - Cell Line
MH  - Chlorocebus aethiops
MH  - Crystallography, X-Ray
MH  - Listeria monocytogenes/*chemistry/metabolism
MH  - Membrane Proteins/*chemistry/metabolism
MH  - Mice
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - *Protein Folding
MH  - Protein Structure, Tertiary
MH  - Proto-Oncogene Proteins c-met/metabolism
MH  - Receptor Protein-Tyrosine Kinases/metabolism
MH  - Repetitive Sequences, Amino Acid
PMC - PMC3083156
EDAT- 2011/02/25 06:00
MHDA- 2011/07/16 06:00
PMCR- 2012/04/29
CRDT- 2011/02/25 06:00
PHST- 2011/02/25 06:00 [entrez]
PHST- 2011/02/25 06:00 [pubmed]
PHST- 2011/07/16 06:00 [medline]
PHST- 2012/04/29 00:00 [pmc-release]
AID - S0021-9258(20)85833-5 [pii]
AID - M110.189951 [pii]
AID - 10.1074/jbc.M110.189951 [doi]
PST - ppublish
SO  - J Biol Chem. 2011 Apr 29;286(17):15496-506. doi: 10.1074/jbc.M110.189951. Epub 
      2011 Feb 23.