4AM9

CRYSTAL STRUCTURE OF THE YERSINIA ENTEROCOLITICA TYPE III SECRETION CHAPERONE SYCD IN COMPLEX WITH A PEPTIDE OF THE TRANSLOCATOR YOPD

Summary for 4AM9

• Entry DOI: 10.2210/pdb4am9/pdb
• Related: 2VGX 2VGY
• Descriptor: CHAPERONE SYCD, YOP EFFECTOR YOPD, SULFATE ION, ... (5 entities in total)
• Functional Keywords: chaperone, chaperone binding domain, chaperone peptide complex, pathogenictiy factor, translocator, tetratricopeptide repeat, tpr, t3ss, virulence factor
• Biological source: YERSINIA ENTEROCOLITICA; More
• Total number of polymer chains: 2
• Total formula weight: 18204.79

Authors

Schreiner, M.,Niemann, H.H. (deposition date: 2012-03-08, release date: 2012-05-30, Last modification date: 2024-11-13)

Primary citation

Schreiner, M.,Niemann, H.H.
Crystal Structure of the Yersinia Enterocolitica Type III Secretion Chaperone Sycd in Complex with a Peptide of the Minor Translocator Yopd
Bmc Struct.Biol., 12:12-, 2012

PubMed Abstract: Type III secretion systems are used by Gram-negative bacteria as "macromolecular syringes" to inject effector proteins into eukaryotic cells. Two hydrophobic proteins called translocators form the necessary pore in the host cell membrane. Both translocators depend on binding to a single chaperone in the bacterial cytoplasm to ensure their stability and efficient transport through the secretion needle. It was suggested that the conserved chaperones bind the more divergent translocators via a hexapeptide motif that is found in both translocators and conserved between species.

PubMed: 22708907
DOI: 10.1186/1472-6807-12-13

Experimental method

X-RAY DIFFRACTION (2.5 Å)